subject:(dehydrogenase)

Portland State University

1. Hannan, Ellen J. A comparison of the effects of fluoride and chloride ions upon the activity of yeast alcohol dehydrogenase.

Degree: MA, Chemistry, 1969, Portland State University

URL: https://pdxscholar.library.pdx.edu/open_access_etds/458

► Very little is known about the effect of hydrofluoric acid and of the fluoride ion on enzyme systems. The purpose of this work was… (more)

Subjects/Keywords: Dehydrogenase

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APA (6^th Edition):

Hannan, E. J. (1969). A comparison of the effects of fluoride and chloride ions upon the activity of yeast alcohol dehydrogenase. (Masters Thesis). Portland State University. Retrieved from https://pdxscholar.library.pdx.edu/open_access_etds/458

Chicago Manual of Style (16^th Edition):

Hannan, Ellen J. “A comparison of the effects of fluoride and chloride ions upon the activity of yeast alcohol dehydrogenase.” 1969. Masters Thesis, Portland State University. Accessed April 15, 2021. https://pdxscholar.library.pdx.edu/open_access_etds/458.

MLA Handbook (7^th Edition):

Hannan, Ellen J. “A comparison of the effects of fluoride and chloride ions upon the activity of yeast alcohol dehydrogenase.” 1969. Web. 15 Apr 2021.

Vancouver:

Hannan EJ. A comparison of the effects of fluoride and chloride ions upon the activity of yeast alcohol dehydrogenase. [Internet] [Masters thesis]. Portland State University; 1969. [cited 2021 Apr 15]. Available from: https://pdxscholar.library.pdx.edu/open_access_etds/458.

Council of Science Editors:

Hannan EJ. A comparison of the effects of fluoride and chloride ions upon the activity of yeast alcohol dehydrogenase. [Masters Thesis]. Portland State University; 1969. Available from: https://pdxscholar.library.pdx.edu/open_access_etds/458

University of California – Riverside

2. Dingwall, Stephanie. Spectroscopic and Mechanistic Studies of the Mo/Cu Carbon Monoxide Dehydrogenase From Oligotropha carboxidovorans.

Degree: Biochemistry and Molecular Biology, 2016, University of California – Riverside

URL: http://www.escholarship.org/uc/item/55d0k225

► The molybdenum- and copper-containing enzyme carbon monoxide dehydrogenase from Oligotropha carboxidovorans catalyzes the oxidation of carbon monoxide to carbon dioxide, bioremediating about 400 million tons… (more)

▼ The molybdenum- and copper-containing enzyme carbon monoxide dehydrogenase from Oligotropha carboxidovorans catalyzes the oxidation of carbon monoxide to carbon dioxide, bioremediating about 400 million tons of CO from the atmosphere annually. During catalysis, the substrate is oxidized at a binuclear metal center containing Mo and Cu, with electrons passed via two [2Fe-2S] clusters to a FAD cofactor before ultimately being transferred to the quinone pool of the electron transport chain. Our studies have examined different aspects of catalysis, from the nature of the electron flow through the system to an examination of the binuclear center during enzyme turnover.First, we have identified the formation of the FADH● semiquinone species during catalysis. This is the first confirmed appearance of the neutral radical species in CO dehydrogenase, revealed from enzyme-monitored turnover, quench flow, and reductive titration experiments.Next, we have determined that pH effects in CO dehydrogenase are unique to the enzyme and associated with its FAD. pH jump and reductive titration experiments at pH 6 and 10 reveal pH-dependent UV/visible spectra. Upon covalent modification of the flavin by diphenyliodonium chloride, which leads to its covalent modification and inactivation at the FAD, spectral differences at the two pH extremes are abolished. Similar experiments involving xanthine oxidase and xanthine dehydrogenase show no pH-dependent spectral differences, implying that the pH effects are unique to CO dehydrogenase.Lastly, electron nuclear double resonance (ENDOR) experiments have been performed to further characterize the binuclear center of the partially-reduced enzyme. ENDOR data of 12C and 13C bicarbonate-bound enzyme reveal that bicarbonate is bound to the copper, rather than the molybdenum of the binuclear center, and so is unlikely to be an intermediate during catalysis. Analysis of 16O and 17O Mims ENDOR indicate that the equatorial ligand in the molybdenum coordination sphere is not a Mo=O but Mo-OH, and is catalytically-labile, being incorporated into the product CO2 and regenerated from solvent in the course of each catalytic sequence.

Subjects/Keywords: Biochemistry; carbon monoxide dehydrogenase; CO dehydrogenase; molybdenum

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APA (6^th Edition):

Dingwall, S. (2016). Spectroscopic and Mechanistic Studies of the Mo/Cu Carbon Monoxide Dehydrogenase From Oligotropha carboxidovorans. (Thesis). University of California – Riverside. Retrieved from http://www.escholarship.org/uc/item/55d0k225

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Dingwall, Stephanie. “Spectroscopic and Mechanistic Studies of the Mo/Cu Carbon Monoxide Dehydrogenase From Oligotropha carboxidovorans.” 2016. Thesis, University of California – Riverside. Accessed April 15, 2021. http://www.escholarship.org/uc/item/55d0k225.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Dingwall, Stephanie. “Spectroscopic and Mechanistic Studies of the Mo/Cu Carbon Monoxide Dehydrogenase From Oligotropha carboxidovorans.” 2016. Web. 15 Apr 2021.

Vancouver:

Dingwall S. Spectroscopic and Mechanistic Studies of the Mo/Cu Carbon Monoxide Dehydrogenase From Oligotropha carboxidovorans. [Internet] [Thesis]. University of California – Riverside; 2016. [cited 2021 Apr 15]. Available from: http://www.escholarship.org/uc/item/55d0k225.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Dingwall S. Spectroscopic and Mechanistic Studies of the Mo/Cu Carbon Monoxide Dehydrogenase From Oligotropha carboxidovorans. [Thesis]. University of California – Riverside; 2016. Available from: http://www.escholarship.org/uc/item/55d0k225

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Victoria

3. Carrington, Yuriko. Biochemistry and evolution of the shikimate dehydrogenase/quinate dehydrogenase gene family in plants.

Degree: Department of Biology, 2020, University of Victoria

URL: http://hdl.handle.net/1828/11791

► Gene duplication and functional diversification is a central driving force in the evolution of plant biochemical diversity. However, the latter process is not well understood.… (more)

Subjects/Keywords: shikimate dehydrogenase; quinate dehydrogenase; shikimate; quinate

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APA (6^th Edition):

Carrington, Y. (2020). Biochemistry and evolution of the shikimate dehydrogenase/quinate dehydrogenase gene family in plants. (Thesis). University of Victoria. Retrieved from http://hdl.handle.net/1828/11791

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Carrington, Yuriko. “Biochemistry and evolution of the shikimate dehydrogenase/quinate dehydrogenase gene family in plants.” 2020. Thesis, University of Victoria. Accessed April 15, 2021. http://hdl.handle.net/1828/11791.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Carrington, Yuriko. “Biochemistry and evolution of the shikimate dehydrogenase/quinate dehydrogenase gene family in plants.” 2020. Web. 15 Apr 2021.

Vancouver:

Carrington Y. Biochemistry and evolution of the shikimate dehydrogenase/quinate dehydrogenase gene family in plants. [Internet] [Thesis]. University of Victoria; 2020. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/1828/11791.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Carrington Y. Biochemistry and evolution of the shikimate dehydrogenase/quinate dehydrogenase gene family in plants. [Thesis]. University of Victoria; 2020. Available from: http://hdl.handle.net/1828/11791

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Portland State University

4. Taylor, Craig David. Physical and kinetic properties of dihydroorotate dehydrogenase from Lactobacillus bulgaricus.

Degree: MS(M.S.) in Biology, Biology, 1969, Portland State University

URL: https://pdxscholar.library.pdx.edu/open_access_etds/62

► Dihydroorotate (DRO) dehydrogenase catalyzes the oxidation of DHO to orotate in the pyrimidine biosynthetic pathway. This enzyme was originally isolated from a bacterium, Zymobacterium… (more)

▼ Dihydroorotate (DRO) dehydrogenase catalyzes the oxidation of DHO to orotate in the pyrimidine biosynthetic pathway. This enzyme was originally isolated from a bacterium, Zymobacterium oroticum, which would ferment orotate as a sole source of energy. This adaptive catabolic enzyme, which catalyzes the reduction of orotate to DRO in an efficient pyridine nucleotide-linked reaction, has been extensively studied by several workers. Until recently, no study has been carried out on the enzyme which catalyzes the reaction in the biosynthetic direction. Preliminary studies have shown that the biosynthetic enzyme in Esherichia coli and a pseudomonad is not capable of reducing orotate to DRO by a pyridine nucleotide-linked reaction. These results suggested that there may be significant differences between the catabolic and biosynthetic enzymes. In the present study biosynthetic DHO dehydrogenase from Lacto-bacillus bulgaricus was investigated on the basis of physical and kinetic properties in order to compare the enzyme with the extensively studied catabolic enzyme. The stoichiometry exhibited by the DHO oxidase activity of the biosynthetic enzyme and the absorption spectrum suggest that biosynthetic DHO dehydrogenase is a flavoprotein. Thin layer chromatography of the flavins extracted from the enzyme and reactivation of apoenzymes specific for flavin mononucleotide or flavin adenine dinucleotide have shown that the enzyme contains flavin mononucleotide. The demonstration of enzyme-catalyzed sulfite autoxidation suggested that iron is present and is involved in electron transport. Inhibitor studies have shown that the enzyme contains sulfhydryl groups and the inactivation of such groups halts internal electron transport early in the sequence. Kinetic studies were carried out including the determination of the Km for dihydroorotate, Ki for orotate, and the pH optimum. The kinetic behavior of the enzyme in the presence of various inhibitors suggest that the essential sulfhydryl groups reside at or near the active site. Ammonium sulfate was found to enhance the activity of the enzyme. Evidence presented suggested that this phenomenon is probably an unspecific anion effect in which the rate constant for the breakdown of the enzyme substrate complex is directly affected. A possible scheme of the internal electron transport of biosynthetic DHO dehydrogenase was presented, using the data from this thesis and additional evidence from studies carried out by other workers on similar enzymes. A summary of the physical and kinetic properties of biosynthetic and catabolic DHO dehydrogenase was presented and a detailed comparison between the two enzymes made.

Subjects/Keywords: Dihydroorotate dehydrogenase; Dehydrogenase

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APA (6^th Edition):

Taylor, C. D. (1969). Physical and kinetic properties of dihydroorotate dehydrogenase from Lactobacillus bulgaricus. (Masters Thesis). Portland State University. Retrieved from https://pdxscholar.library.pdx.edu/open_access_etds/62

Chicago Manual of Style (16^th Edition):

Taylor, Craig David. “Physical and kinetic properties of dihydroorotate dehydrogenase from Lactobacillus bulgaricus.” 1969. Masters Thesis, Portland State University. Accessed April 15, 2021. https://pdxscholar.library.pdx.edu/open_access_etds/62.

MLA Handbook (7^th Edition):

Taylor, Craig David. “Physical and kinetic properties of dihydroorotate dehydrogenase from Lactobacillus bulgaricus.” 1969. Web. 15 Apr 2021.

Vancouver:

Taylor CD. Physical and kinetic properties of dihydroorotate dehydrogenase from Lactobacillus bulgaricus. [Internet] [Masters thesis]. Portland State University; 1969. [cited 2021 Apr 15]. Available from: https://pdxscholar.library.pdx.edu/open_access_etds/62.

Council of Science Editors:

Taylor CD. Physical and kinetic properties of dihydroorotate dehydrogenase from Lactobacillus bulgaricus. [Masters Thesis]. Portland State University; 1969. Available from: https://pdxscholar.library.pdx.edu/open_access_etds/62

5. Figueroa-Teran, Rubi D. Ipsdienol Dehydrogenase (IDOLDH), a Novel Oxidoreductase Important in the Last Steps of Pheromone Biosynthesis in Ips Spp. (Coleoptera: Scolytinae: Curculionidae).

Degree: 2011, University of Nevada – Reno

URL: http://hdl.handle.net/11714/3927

► Ips spp. beetles biosynthesize ipsdienol and ipsenol in different enantiomeric blends and ratios as pheromones. In order to understand how these beetles evolved the ability… (more)

▼ Ips spp. beetles biosynthesize ipsdienol and ipsenol in different enantiomeric blends and ratios as pheromones. In order to understand how these beetles evolved the ability to use the same components to synthesize different pheromone blends, the last steps of ipsdienol and ipsenol biosynthesis, which are probably catalyzed by oxidoreductases, must be characterized. Here I report the isolation of ipsdienol dehydrogenase (IDOLDH) from the three bark beetles (Coleoptera): western Ips pini (wIDOLDH), I. confusus (IcIDOLDH) and eastern I. pini (eIpIDOLDH). IDOLDH is the first characterized non-dipteran insect monoterpene short-chain dehydrogenase/reductase (SDR). Quantitative real-time PCR experiments showed that wIDOLDH transcript was induced by feeding in male midguts, the hallmark of pheromone biosynthetic genes. Surprisingly, protein levels were unaffected by feeding, suggesting other factor(s) control pheromone biosynthesis. IDOLDH was present only in male midguts, not in females or other tissues. Functional characterization of wIDOLDH and IcIDOLDH provide the first direct evidence for ipsenol biosynthesis through ketone intermediates and interconversion of (-)-ipsdienol to ipsdienone. WIpIDOLDH oxidized racemic and (-)-ipsdienol to ipsdienone and reduced ipsdienone to (-)-ipsdienol and ipsenone to (-)-ipsenol, but discriminated against (+)- ipsdienol as a substrate. IcIDOLDH similarly oxidized (-)-ipsdienol to ipsdienone, discriminated against (+)-ipsdienol, reduced ipsdienone to ipsdienol (stereochemistry not determined), and used ipsenone as a substrate. Ongoing studies showed eIpIDOLDH had similar activities. Kinetic analysis of IDOLDH oxidation of (-)-ipsdienol with NADP⁺ followed the Michaelis-Menton model, indicating this type of analysis is adequate to characterize IDOLDH catalyzed reactions. The expression profiles and conservation of activities across three species strongly supports that IDOLDH has evolved specifically for pheromone biosynthesis in Ips beetles. The functional data indicates that IDOLDH contributes to, but does not solely control the enantiomeric blend of ipsdienol in Ips spp. Additionally, ipsenone was not a reduction product of ipsdienone, suggesting an ipsenone reductase (IDONER) is required for ipsenone biosynthesis. IDOLDH’s primary structure contains all the critical motifs of an alcohol dehydrogenase in the SDR superfamily. Primary sequence identity of IDOLDH isozymes was not as high as expected for sibling species (82%), however the substrate binding loop was highly identical (99%) and the fact that they retain similar substrate profiles suggest that the differences are not important in determining function. Primary sequence comparisons with the human L-3-hydroxyacyl-CoA dehydrogenase type II/ amyloid-β binding alcohol dehydrogenase (hHADH II/ ABAD) showed a much lower identity (36%) but was still surprisingly high for such diverse organisms with different substrate preferences. Although the overall architecture of these enzymes is similar the … Advisors/Committee Members: Tittiger, Claus R. (advisor), Welch, William (committee member), Blomquist, Gary J. (committee member), Shintani, David (committee member), Berninsone, Patricia (committee member).

Subjects/Keywords: Bark Beetles; Ipsdienol dehydrogenase; Ips pini; monoterpene dehydrogenase; Pheromone; Short chain dehydrogenase/reductase (SDR)

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APA (6^th Edition):

Figueroa-Teran, R. D. (2011). Ipsdienol Dehydrogenase (IDOLDH), a Novel Oxidoreductase Important in the Last Steps of Pheromone Biosynthesis in Ips Spp. (Coleoptera: Scolytinae: Curculionidae). (Thesis). University of Nevada – Reno. Retrieved from http://hdl.handle.net/11714/3927

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Figueroa-Teran, Rubi D. “Ipsdienol Dehydrogenase (IDOLDH), a Novel Oxidoreductase Important in the Last Steps of Pheromone Biosynthesis in Ips Spp. (Coleoptera: Scolytinae: Curculionidae).” 2011. Thesis, University of Nevada – Reno. Accessed April 15, 2021. http://hdl.handle.net/11714/3927.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Figueroa-Teran, Rubi D. “Ipsdienol Dehydrogenase (IDOLDH), a Novel Oxidoreductase Important in the Last Steps of Pheromone Biosynthesis in Ips Spp. (Coleoptera: Scolytinae: Curculionidae).” 2011. Web. 15 Apr 2021.

Vancouver:

Figueroa-Teran RD. Ipsdienol Dehydrogenase (IDOLDH), a Novel Oxidoreductase Important in the Last Steps of Pheromone Biosynthesis in Ips Spp. (Coleoptera: Scolytinae: Curculionidae). [Internet] [Thesis]. University of Nevada – Reno; 2011. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/11714/3927.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Figueroa-Teran RD. Ipsdienol Dehydrogenase (IDOLDH), a Novel Oxidoreductase Important in the Last Steps of Pheromone Biosynthesis in Ips Spp. (Coleoptera: Scolytinae: Curculionidae). [Thesis]. University of Nevada – Reno; 2011. Available from: http://hdl.handle.net/11714/3927

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Utah

6. Hennebold, Jon Douglas. Regulation of steroid hormone action in lymphoid organs.

Degree: PhD, Pathology;, 1996, University of Utah

URL: http://content.lib.utah.edu/cdm/singleitem/collection/etd2/id/179/rec/967

► The neuroendocrine system regulates a variety of lymphoid cell activities through the actions of steroid hormones, including dehydroepiandrosterone (DHEA) and the glucocorticoids (GCS). This provides… (more)

▼ The neuroendocrine system regulates a variety of lymphoid cell activities through the actions of steroid hormones, including dehydroepiandrosterone (DHEA) and the glucocorticoids (GCS). This provides a linkage between the neuroendocrine and immune systems through the autocrine, paracrine, and endocrine acting substances that are produced. The studies in this thesis describe the mechanisms utilized by the lymphoid system to microenvironmentally control the immunomodulatory actions of DHEA and GCS in vivo. In the circulation, DHEA exists predominantly as the hydrophilic sulfated derivative dehydroepiandrosterone sulfate (DHEAS). The enzyme DHEAS sulfatase generates DHEA through the hydrolysis of the 3-beta-sulfate group. The DHEA that is formed from this enzymatic process is hydrophobic and effectively diffuses across cellular membranes. High levels of DHEAS sulfatase activity were observed within lymphoid organs, and predominantly associates with the macrophage. Stimulation of macrophages with a variety of microbial substances markedly inhibited the conversion of DHEAS to DHEA. Inhibition of enzyme activity was determined to be mediated by the actions of the macrophage synthesized cytokines TNF-alpha and IFN-alpha. Lymphoid organs were found to possess substantial levels of the enzyme 11-beta-hydroxysteroid dehydrogenase (11-beta-HSD). This enzyme interconverts the biologically active 11-hydroxy GCS to their biologically inactive 11-keto metabolites. Enzyme activity was found to vary within distinct lymphoid organs and associate with the immobile stromal elements. Physical and enzymological properties of the 11-beta-HSD activity present within lymphoid organs differed from the properties described for the two recently cloned and characterized 11-beta-HSD1 and 11-beta-HSD2 isoforms, suggesting the existence within these tissues of a novel 11-beta-HSD isoform. Inhibition of lymphoid organ 11-beta-HSD activity in vivo resulted in altered immune effector functions. This included a reduction in the production of activation inducible pro-inflammatory cytokines plus a depression in cell mediated immune responses. Similar effects are observed following the exogenous administration of GCS. These findings indicate that 11-beta-HSD within lymphoid organs and other tissues control the capacity of the GCS to function as immunomodulatory substances.

Subjects/Keywords: Enzymes; Dehydrogenase

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APA (6^th Edition):

Hennebold, J. D. (1996). Regulation of steroid hormone action in lymphoid organs. (Doctoral Dissertation). University of Utah. Retrieved from http://content.lib.utah.edu/cdm/singleitem/collection/etd2/id/179/rec/967

Chicago Manual of Style (16^th Edition):

Hennebold, Jon Douglas. “Regulation of steroid hormone action in lymphoid organs.” 1996. Doctoral Dissertation, University of Utah. Accessed April 15, 2021. http://content.lib.utah.edu/cdm/singleitem/collection/etd2/id/179/rec/967.

MLA Handbook (7^th Edition):

Hennebold, Jon Douglas. “Regulation of steroid hormone action in lymphoid organs.” 1996. Web. 15 Apr 2021.

Vancouver:

Hennebold JD. Regulation of steroid hormone action in lymphoid organs. [Internet] [Doctoral dissertation]. University of Utah; 1996. [cited 2021 Apr 15]. Available from: http://content.lib.utah.edu/cdm/singleitem/collection/etd2/id/179/rec/967.

Council of Science Editors:

Hennebold JD. Regulation of steroid hormone action in lymphoid organs. [Doctoral Dissertation]. University of Utah; 1996. Available from: http://content.lib.utah.edu/cdm/singleitem/collection/etd2/id/179/rec/967

University of Waikato

7. Prentice, Erica Jean. Characterisation of Enzyme Evolution through Ancestral Enzyme Reconstruction .

Degree: 2013, University of Waikato

URL: http://hdl.handle.net/10289/8717

► Through ancestral sequence reconstruction (ASR) techniques, ancient enzymes can be recreated and biochemically tested, giving insight into the enzymes’ evolutionary history. A previous study by… (more)

▼ Through ancestral sequence reconstruction (ASR) techniques, ancient enzymes can be recreated and biochemically tested, giving insight into the enzymes’ evolutionary history. A previous study by Hobbs et al. (2012) has shown that some ancestral 3-isopropylmalate dehydrogenase (IPMDH) enzymes of the Bacillus lineage are more catalytically efficient and kinetically stable than extant counterparts. Given these characteristics, this trend raises questions as to why ancestral Bacillus IPMDH enzymes have been superseded by catalytically slower and less kinetically stable counterparts. The homology between IPMDH and the dehydrogenases of tartrate, malate and isocitrate makes IPMDH an interesting model enzyme in terms of the evolution of substrate specificity. Here, the reconstruction of a 2.7 billion year old enzyme has been attempted to extend the reconstruction of IPMDH back to the last common ancestor of the Firmicutes. This reconstruction tested the limits of ASR techniques in terms of time and levels of sequence divergence, especially for such a structurally complex enzyme. However, upon expression and purification, the enzyme was found to form an inactive, soluble aggregate. This suggests that current ASR techniques are too simplistic to reconstruct the complexity and divergence of IPMDH back as far as the last common ancestor of the Firmicutes. Enzyme evolution was investigated with ancestors from the Bacillus genus. Substrate promiscuity of ancestral enzymes was compared to a contemporary counterpart. It was concluded that the ancestral IPMDH enzymes tested do not show additional substrate promiscuity when compared to contemporary counterparts. The fitness of organisms carrying the IPMDH ancestors was assessed to establish what effects the high turnover rates and kinetic stability possessed by some ancestral IPMDH enzymes had on cells when functioning within the normal catalytic pathway for leucine. In vivo, the fastest and most kinetically stable ancestral IPMDH resulted in slower growth rates. This detrimental effect in vivo clarifies why this enzyme has been lost over evolutionary time. The X-ray crystal structure of the most recent IPMDH ancestor was also determined at 2.6 Å resolution. The structure of this ancestral IPMDH was found to be similar to other IPMDH structures, including the previously solved IPMDH from the last common ancestor of the Bacillus. Advisors/Committee Members: Arcus, Vickery L (advisor).

Subjects/Keywords: ancestral sequence reconstructio; isopropylmalate dehydrogenase

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APA (6^th Edition):

Prentice, E. J. (2013). Characterisation of Enzyme Evolution through Ancestral Enzyme Reconstruction . (Masters Thesis). University of Waikato. Retrieved from http://hdl.handle.net/10289/8717

Chicago Manual of Style (16^th Edition):

Prentice, Erica Jean. “Characterisation of Enzyme Evolution through Ancestral Enzyme Reconstruction .” 2013. Masters Thesis, University of Waikato. Accessed April 15, 2021. http://hdl.handle.net/10289/8717.

MLA Handbook (7^th Edition):

Prentice, Erica Jean. “Characterisation of Enzyme Evolution through Ancestral Enzyme Reconstruction .” 2013. Web. 15 Apr 2021.

Vancouver:

Prentice EJ. Characterisation of Enzyme Evolution through Ancestral Enzyme Reconstruction . [Internet] [Masters thesis]. University of Waikato; 2013. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10289/8717.

Council of Science Editors:

Prentice EJ. Characterisation of Enzyme Evolution through Ancestral Enzyme Reconstruction . [Masters Thesis]. University of Waikato; 2013. Available from: http://hdl.handle.net/10289/8717

Oregon State University

8. Lu, Fung-jou. The effect of coenzyme on the bis(1-anilino-8-naphthalenesulfonate) induced association of lactic dehydrogenase.

Degree: MS, Biochemistry and Biophysics, 1972, Oregon State University

URL: http://hdl.handle.net/1957/46112

Subjects/Keywords: Lactate dehydrogenase

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APA (6^th Edition):

Lu, F. (1972). The effect of coenzyme on the bis(1-anilino-8-naphthalenesulfonate) induced association of lactic dehydrogenase. (Masters Thesis). Oregon State University. Retrieved from http://hdl.handle.net/1957/46112

Chicago Manual of Style (16^th Edition):

Lu, Fung-jou. “The effect of coenzyme on the bis(1-anilino-8-naphthalenesulfonate) induced association of lactic dehydrogenase.” 1972. Masters Thesis, Oregon State University. Accessed April 15, 2021. http://hdl.handle.net/1957/46112.

MLA Handbook (7^th Edition):

Lu, Fung-jou. “The effect of coenzyme on the bis(1-anilino-8-naphthalenesulfonate) induced association of lactic dehydrogenase.” 1972. Web. 15 Apr 2021.

Vancouver:

Lu F. The effect of coenzyme on the bis(1-anilino-8-naphthalenesulfonate) induced association of lactic dehydrogenase. [Internet] [Masters thesis]. Oregon State University; 1972. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/1957/46112.

Council of Science Editors:

Lu F. The effect of coenzyme on the bis(1-anilino-8-naphthalenesulfonate) induced association of lactic dehydrogenase. [Masters Thesis]. Oregon State University; 1972. Available from: http://hdl.handle.net/1957/46112

Queens University

9. Elharram, Ahmed. Assessing Memory in an Aldehyde Dehydrogenase 2 Knockout Model of Alzheimer's Disease .

Degree: Pharmacology and Toxicology, 2013, Queens University

URL: http://hdl.handle.net/1974/8335

► The study of Alzheimer’s Disease (AD) has been hindered by the absence of animal models of late-onset/age-related AD (also termed sporadic AD) (95% of AD… (more)

Subjects/Keywords: Alzheimer's ; Aldehyde Dehydrogenase 2 ; Memory

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APA (6^th Edition):

Elharram, A. (2013). Assessing Memory in an Aldehyde Dehydrogenase 2 Knockout Model of Alzheimer's Disease . (Thesis). Queens University. Retrieved from http://hdl.handle.net/1974/8335

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Elharram, Ahmed. “Assessing Memory in an Aldehyde Dehydrogenase 2 Knockout Model of Alzheimer's Disease .” 2013. Thesis, Queens University. Accessed April 15, 2021. http://hdl.handle.net/1974/8335.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Elharram, Ahmed. “Assessing Memory in an Aldehyde Dehydrogenase 2 Knockout Model of Alzheimer's Disease .” 2013. Web. 15 Apr 2021.

Vancouver:

Elharram A. Assessing Memory in an Aldehyde Dehydrogenase 2 Knockout Model of Alzheimer's Disease . [Internet] [Thesis]. Queens University; 2013. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/1974/8335.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Elharram A. Assessing Memory in an Aldehyde Dehydrogenase 2 Knockout Model of Alzheimer's Disease . [Thesis]. Queens University; 2013. Available from: http://hdl.handle.net/1974/8335

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Massey University

10. Harvey, Jacqueline Jean. Laser light scattering and ultracentrifuge studies on sheep liver cytosolic aldehyde dehydrogenase.

Degree: MS, Chemistry, 1995, Massey University

URL: http://hdl.handle.net/10179/12876

► The techniques of laser light scattering and ultracentrifugation were used to investigate the association - dissociation behaviour of sheep liver cytosolic aldehyde dehydrogenase. Diffusion and… (more)

Subjects/Keywords: Aldehyde dehydrogenase

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APA (6^th Edition):

Harvey, J. J. (1995). Laser light scattering and ultracentrifuge studies on sheep liver cytosolic aldehyde dehydrogenase. (Masters Thesis). Massey University. Retrieved from http://hdl.handle.net/10179/12876

Chicago Manual of Style (16^th Edition):

Harvey, Jacqueline Jean. “Laser light scattering and ultracentrifuge studies on sheep liver cytosolic aldehyde dehydrogenase.” 1995. Masters Thesis, Massey University. Accessed April 15, 2021. http://hdl.handle.net/10179/12876.

MLA Handbook (7^th Edition):

Harvey, Jacqueline Jean. “Laser light scattering and ultracentrifuge studies on sheep liver cytosolic aldehyde dehydrogenase.” 1995. Web. 15 Apr 2021.

Vancouver:

Harvey JJ. Laser light scattering and ultracentrifuge studies on sheep liver cytosolic aldehyde dehydrogenase. [Internet] [Masters thesis]. Massey University; 1995. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10179/12876.

Council of Science Editors:

Harvey JJ. Laser light scattering and ultracentrifuge studies on sheep liver cytosolic aldehyde dehydrogenase. [Masters Thesis]. Massey University; 1995. Available from: http://hdl.handle.net/10179/12876

University of British Columbia

11. Norberg, Carol Louise. Temperature and pressure adaptations of substrate and coenzyme binding by M4 lactate dehydrogenase.

Degree: MS- MSc, Zoology, 1975, University of British Columbia

URL: http://hdl.handle.net/2429/19793

► Lactate dehydrogenases from an abyssal fish, a dogfish, a tidepool sculpin, and a mammal have been found to differ in their ability to bind substrate… (more)

▼ Lactate dehydrogenases from an abyssal fish, a dogfish, a tidepool sculpin, and a mammal have been found to differ in their ability to bind substrate analog and coenzyme at varying temperatures and pressures. Affinities for a substrate analog are quite similar for each lactate dehydrogenase at their respective biological temperatures, suggesting temperature-dependent modification of enzyme-substrate binding for optimal function. Binding of coenzyme by the three ectothermic enzymes is less affected by changes in temperature than is coenzyme binding by the mammalian enzyme, and coenzyme binding by the abyssal fish enzyme is considerably less sensitive to high hydrostatic pressure than it is in the case of the other three lactate dehydrogenases. The total free energy change involved in binding coenzyme and substrate analog is only slightly higher for the endothermic than for the three ectothermic enzymes, but the enthalpic and entropic contributions are quite different. The ectotherms appear to have minimized the enthalpic contribution and hence minimized temperature effects on binding. The relationship between enthalpy and entropy for each of the binding interactions studied is a straight line of slope within the limits found by other workers for water-solute interactions and/or weak bond formation and is presumed to be a result of the conformational changes accompanying ligand binding. The contributions to binding of the AMP and nicotinamide subsites of the coenzyme binding site give a good estimate of many of the binding interactions of the coenzyme as a whole, and appear to compensate one another to maintain low AH and AS values for coenzyme binding to the ectothermic enzymes. This same type of compensation in volume change can be seen between the substrate and coenzyme binding sites for the abyssal fish lactate dehydrogenase, resulting in a net volume change very close to zero. The observed temperature and pressure effects on binding cannot be explained solely in terms of the types of weak bonds involved, and known homologies between dogfish and pig LDH make major differences between the active sites unlikely. Conformational changes occurring simultaneously with binding may be of considerable importance in modifying the observed responses to both temperature and pressure.

Subjects/Keywords: Lactate dehydrogenase

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APA (6^th Edition):

Norberg, C. L. (1975). Temperature and pressure adaptations of substrate and coenzyme binding by M4 lactate dehydrogenase. (Masters Thesis). University of British Columbia. Retrieved from http://hdl.handle.net/2429/19793

Chicago Manual of Style (16^th Edition):

Norberg, Carol Louise. “Temperature and pressure adaptations of substrate and coenzyme binding by M4 lactate dehydrogenase.” 1975. Masters Thesis, University of British Columbia. Accessed April 15, 2021. http://hdl.handle.net/2429/19793.

MLA Handbook (7^th Edition):

Norberg, Carol Louise. “Temperature and pressure adaptations of substrate and coenzyme binding by M4 lactate dehydrogenase.” 1975. Web. 15 Apr 2021.

Vancouver:

Norberg CL. Temperature and pressure adaptations of substrate and coenzyme binding by M4 lactate dehydrogenase. [Internet] [Masters thesis]. University of British Columbia; 1975. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/2429/19793.

Council of Science Editors:

Norberg CL. Temperature and pressure adaptations of substrate and coenzyme binding by M4 lactate dehydrogenase. [Masters Thesis]. University of British Columbia; 1975. Available from: http://hdl.handle.net/2429/19793

Michigan State University

12. Burdette, Douglas S. Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase : molecular basis for stability and catalysis.

Degree: PhD, Department of Biochemistry, 1996, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:29990

Subjects/Keywords: Alcohol dehydrogenase

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APA (6^th Edition):

Burdette, D. S. (1996). Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase : molecular basis for stability and catalysis. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:29990

Chicago Manual of Style (16^th Edition):

Burdette, Douglas S. “Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase : molecular basis for stability and catalysis.” 1996. Doctoral Dissertation, Michigan State University. Accessed April 15, 2021. http://etd.lib.msu.edu/islandora/object/etd:29990.

MLA Handbook (7^th Edition):

Burdette, Douglas S. “Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase : molecular basis for stability and catalysis.” 1996. Web. 15 Apr 2021.

Vancouver:

Burdette DS. Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase : molecular basis for stability and catalysis. [Internet] [Doctoral dissertation]. Michigan State University; 1996. [cited 2021 Apr 15]. Available from: http://etd.lib.msu.edu/islandora/object/etd:29990.

Council of Science Editors:

Burdette DS. Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase : molecular basis for stability and catalysis. [Doctoral Dissertation]. Michigan State University; 1996. Available from: http://etd.lib.msu.edu/islandora/object/etd:29990

University of Sydney

13. Cho, Angela. Biomarkers of progression and recurrence in IDH mutated gliomas .

Degree: 2020, University of Sydney

URL: http://hdl.handle.net/2123/24611

► Gliomas are the most common primary brain tumours in adults. Mutations in Isocitrate Dehydrogenase 1 and 2 (IDH1/2) define a glioma subtype with a better… (more)

▼ Gliomas are the most common primary brain tumours in adults. Mutations in Isocitrate Dehydrogenase 1 and 2 (IDH1/2) define a glioma subtype with a better prognosis than its wildtype counterpart. Although IDH mutant low grade gliomas (LGGs) have a relatively indolent clinical course, recurrence and progression to a higher grade are inevitable. A major challenge in neuro-oncology is the management of LGGs which have progressed as there is no standard treatment of care. Monitoring glioma progression and response to treatment is critical for patient management and is currently performed by imaging. However, inflammatory responses can mimic progression, and this pseudoprogression hinders accurate prognostication. In this thesis, circulating tumour DNA (ctDNA) and RNA from tumour-educated platelets were assessed as biomarker sources for monitoring patients with IDH1 R132H gliomas. OMICs analysis of matched IDH mutant low grade and progressed astrocytomas was undertaken to identify factors driving glioma progression and recurrence. Identified factors were assessed in independent cohorts for their prognostic potential. Droplet digital PCR assays were established for detection of IDH1 wildtype and R132H transcript and DNA. While these exhibited high specificities, the sensitivities were not sufficient for robust detection of circulating mutant molecules from patients with IDH1 R132H gliomas. OMICs analysis revealed decreased differentiation and increased mesenchymal and immunosuppressive features in recurrent higher-grade IDH mutant astrocytomas. Carboxypeptidase E was validated as an independent positive predictor of overall survival (OS) for patients with IDH mutant astrocytomas. A 3-protein panel was validated as a strong independent negative predictor of OS in patients with astrocytomas. This research increased understanding of IDH mutant astrocytoma progression and identified novel biomarkers with the potential for improved prognostication and monitoring of astrocytomas.

Subjects/Keywords: glioma; isocitrate dehydrogenase; IDH

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APA (6^th Edition):

Cho, A. (2020). Biomarkers of progression and recurrence in IDH mutated gliomas . (Thesis). University of Sydney. Retrieved from http://hdl.handle.net/2123/24611

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Cho, Angela. “Biomarkers of progression and recurrence in IDH mutated gliomas .” 2020. Thesis, University of Sydney. Accessed April 15, 2021. http://hdl.handle.net/2123/24611.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Cho, Angela. “Biomarkers of progression and recurrence in IDH mutated gliomas .” 2020. Web. 15 Apr 2021.

Vancouver:

Cho A. Biomarkers of progression and recurrence in IDH mutated gliomas . [Internet] [Thesis]. University of Sydney; 2020. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/2123/24611.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Cho A. Biomarkers of progression and recurrence in IDH mutated gliomas . [Thesis]. University of Sydney; 2020. Available from: http://hdl.handle.net/2123/24611

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Saskatchewan

14. Bertwistle, Drew. X-ray Crystallography of Inositol Dehydrogenase Enzymes.

Degree: 2015, University of Saskatchewan

URL: http://hdl.handle.net/10388/ETD-2015-04-2027

► Lactobacillus casei BL23 expresses two enzymes encoded by the genes iolG1 and iolG2. They have been putatively assigned as myo-inositol dehydrogenases by sequence comparison. The… (more)

Subjects/Keywords: X-ray Crystallography; myo-inositol dehydrogenase; scyllo-inositol dehydrogenase; structural biology

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APA (6^th Edition):

Bertwistle, D. (2015). X-ray Crystallography of Inositol Dehydrogenase Enzymes. (Thesis). University of Saskatchewan. Retrieved from http://hdl.handle.net/10388/ETD-2015-04-2027

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Bertwistle, Drew. “X-ray Crystallography of Inositol Dehydrogenase Enzymes.” 2015. Thesis, University of Saskatchewan. Accessed April 15, 2021. http://hdl.handle.net/10388/ETD-2015-04-2027.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Bertwistle, Drew. “X-ray Crystallography of Inositol Dehydrogenase Enzymes.” 2015. Web. 15 Apr 2021.

Vancouver:

Bertwistle D. X-ray Crystallography of Inositol Dehydrogenase Enzymes. [Internet] [Thesis]. University of Saskatchewan; 2015. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10388/ETD-2015-04-2027.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Bertwistle D. X-ray Crystallography of Inositol Dehydrogenase Enzymes. [Thesis]. University of Saskatchewan; 2015. Available from: http://hdl.handle.net/10388/ETD-2015-04-2027

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Otago

15. McNeil, Matthew Brad. Characterisation of the conserved hypothetical proteins SdhE and YgfX in Serratia 39006 .

Degree: 2012, University of Otago

URL: http://hdl.handle.net/10523/2373

► Serratia sp. ATCC 39006 (Serratia 39006) is a Gram-negative bacterium from the Enterobacteriaceae family. Serratia 39006 is able to produce a number of secondary metabolites… (more)

▼ Serratia sp. ATCC 39006 (Serratia 39006) is a Gram-negative bacterium from the Enterobacteriaceae family. Serratia 39006 is able to produce a number of secondary metabolites including the red tripyrrole antibiotic prodigiosin (pig). Although the physiological role of pig remains unknown it is of considerable clinical interest due to its immunosuppressive and anti-cancer properties. Furthermore, a complex hierarchy involving a network of regulatory proteins allows pig biosynthesis to be regulated by multiple environmental inputs. Conserved hypothetical proteins are of unknown function and account for approximately 30% of all proteins in eukaryotic and bacterial genomes. Two conserved hypothetical proteins, termed SdhE and YgfX, were previously identified as positive regulators of pig biosynthesis. In an attempt to further understand how SdhE and YgfX regulate pig biosynthesis this investigation has utilised a combination of bioinformatic, genetic and biochemical techniques. SdhE is a highly conserved protein present in both eukaryotes and bacteria. Investigations revealed that it was required for the activity of succinate dehydrogenase, an important component of the electron transport chain and tricarboxylic acid cycle. SdhE interacted with the flavoprotein subunit SdhA, directly bound the flavin adenine dinucleotide (FAD) cofactor and was required for the flavinylation of SdhA. This is the first demonstration of a protein required for FAD incorporation in bacteria. YgfX is a membrane bound protein that is able to multimerise. YgfX also directly interacted with SdhE suggesting that it may regulate the activity of SdhE at a post-transcriptional level or alternatively that SdhE may regulate YgfX. In conclusion, the characterisation of SdhE in this study has identified a novel biochemical function important for bacterial metabolism. Furthermore, the functional linkage between SdhE and YgfX provides a new regulatory pathway linking cellular metabolism and pig biosynthesis. Advisors/Committee Members: Fineran, Peter Charles (advisor).

Subjects/Keywords: Prodigiosin; FAD; SdhE; YgfX; Succinate dehydrogenase; SdhA

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APA (6^th Edition):

McNeil, M. B. (2012). Characterisation of the conserved hypothetical proteins SdhE and YgfX in Serratia 39006 . (Doctoral Dissertation). University of Otago. Retrieved from http://hdl.handle.net/10523/2373

Chicago Manual of Style (16^th Edition):

McNeil, Matthew Brad. “Characterisation of the conserved hypothetical proteins SdhE and YgfX in Serratia 39006 .” 2012. Doctoral Dissertation, University of Otago. Accessed April 15, 2021. http://hdl.handle.net/10523/2373.

MLA Handbook (7^th Edition):

McNeil, Matthew Brad. “Characterisation of the conserved hypothetical proteins SdhE and YgfX in Serratia 39006 .” 2012. Web. 15 Apr 2021.

Vancouver:

McNeil MB. Characterisation of the conserved hypothetical proteins SdhE and YgfX in Serratia 39006 . [Internet] [Doctoral dissertation]. University of Otago; 2012. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10523/2373.

Council of Science Editors:

McNeil MB. Characterisation of the conserved hypothetical proteins SdhE and YgfX in Serratia 39006 . [Doctoral Dissertation]. University of Otago; 2012. Available from: http://hdl.handle.net/10523/2373

Ruhr Universität Bochum

16. Shao, Minling. Design of efficient electron transfer pathways for enzymatic biofuel cell anodes.

Degree: 2013, Ruhr Universität Bochum

URL: http://nbn-resolving.de/urn/resolver.pl?urn=urn:nbn:de:hbz:294-36533

► Enzymatische Biobrennstoffzellen (EBFCs) sind wegen ihrer potentiellen Anwendung als implantierbare Energiequelle bzw. als Batterieersatz in den letzten Jahren immer stärker in den Fokus der Forschung… (more)

Subjects/Keywords: Cellobiose-Dehydrogenase; Sauerstoff; Osmium; Mediator; Elektrochemie

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APA (6^th Edition):

Shao, M. (2013). Design of efficient electron transfer pathways for enzymatic biofuel cell anodes. (Thesis). Ruhr Universität Bochum. Retrieved from http://nbn-resolving.de/urn/resolver.pl?urn=urn:nbn:de:hbz:294-36533

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Shao, Minling. “Design of efficient electron transfer pathways for enzymatic biofuel cell anodes.” 2013. Thesis, Ruhr Universität Bochum. Accessed April 15, 2021. http://nbn-resolving.de/urn/resolver.pl?urn=urn:nbn:de:hbz:294-36533.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Shao, Minling. “Design of efficient electron transfer pathways for enzymatic biofuel cell anodes.” 2013. Web. 15 Apr 2021.

Vancouver:

Shao M. Design of efficient electron transfer pathways for enzymatic biofuel cell anodes. [Internet] [Thesis]. Ruhr Universität Bochum; 2013. [cited 2021 Apr 15]. Available from: http://nbn-resolving.de/urn/resolver.pl?urn=urn:nbn:de:hbz:294-36533.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Shao M. Design of efficient electron transfer pathways for enzymatic biofuel cell anodes. [Thesis]. Ruhr Universität Bochum; 2013. Available from: http://nbn-resolving.de/urn/resolver.pl?urn=urn:nbn:de:hbz:294-36533

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Otago

17. Ekanayaka, Nandula Vidumini. Growth and Energetics of Cholesterol Utilisation by Mycobacterium smegmatis mc2155 .

Degree: 2013, University of Otago

URL: http://hdl.handle.net/10523/3743

► Members of the genus Mycobacterium are able to degrade cholesterol and for pathogenic members like Mycobacterium tuberculosis this degradation has been implicated in persistence in… (more)

▼ Members of the genus Mycobacterium are able to degrade cholesterol and for pathogenic members like Mycobacterium tuberculosis this degradation has been implicated in persistence in the lungs of the chronically infected host. The physiological role of cholesterol and the enzymes involved in its breakdown by mycobacteria requires further investigation. The aims of this thesis were to determine how Mycobacterium smegmatis degrades cholesterol and identify the genetic components involved in this degradation. To address this goal, I studied the transcriptional response of M. smegmatis mc2155 to cholesterol (compared to glycerol) at very low growth rate (i.e. ~ 69 h doubling time) using continuous culture and microarray analysis. M. smegmatis was able to utilise cholesterol as a sole carbon and energy source at low growth rate. During growth in continuous culture, 75 µM cholesterol remained in the medium suggesting that M. smegmatis did not use an active transport system to accumulate cholesterol from this medium. This was confirmed by transport studies using [4-14C]-cholesterol. Microarray analysis revealed 243 genes upregulated and 269 genes downregulated when grown on cholesterol compared to glycerol (p-value ≤ 0.1). The majority of these genes encoded hypothetical proteins. Genes implicated in a cholesterol degradation pathway were significantly upregulated (p-value ≤ 0.1). Clusters of genes in the KstR and KstR2 lipid degradation regulons were upregulated along with four lipid-transfer proteins some of which have previously been shown to be essential for intracellular survival of M. tuberculosis. Comparing the cholesterol and hypoxia transcriptomes revealed a 35 % overlap, but also a large cholesterol-specific set of genes were present and are collectively designated as the cholesterol specific transcriptome in this study. The expression of a putative lysine exporter (lysE; MSMEG_0467) was upregulated 28-fold along with the downregulation (50-fold) of an enzyme involved in lysine transamination (L-lysine-ε-aminotransferase; MSMEG_1764) indicating accumulation and export of lysine during growth on cholesterol. We propose that lysine export may represent a novel “overflow” metabolism during growth on cholesterol as a ∆lysE mutant of M. smegmatis showed impaired growth on cholesterol and other fatty acids, but not on glycerol or glucose (Berney, Ekanayaka and Cook, unpublished data). During growth on cholesterol, there was a concurrent induction of the glyoxylate shunt, the methylcitrate cycle and the methylmalonate pathway, which results in an increased flux towards succinate and this was reflected by the significant upregulation of one of the two annotated succinate dehydrogenase gene clusters (Sdh2) of M. smegmatis. Whereas the second annotated succinate dehydrogenase operon (Sdh1) was significantly downregulated. Sdh1 was encoded in an operon of five genes (MSMEG_0420 to 0416) and Sdh2 was encoded in an operon of four genes (MSMEG_1672 to 1669) as confirmed by RT-PCR. Using 5’RACE analysis the transcriptional start… Advisors/Committee Members: Cook, Gregory (advisor).

Subjects/Keywords: Mycobacteria; cholesterol; succinate dehydrogenase; continuous culture; microarray

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APA (6^th Edition):

Ekanayaka, N. V. (2013). Growth and Energetics of Cholesterol Utilisation by Mycobacterium smegmatis mc2155 . (Doctoral Dissertation). University of Otago. Retrieved from http://hdl.handle.net/10523/3743

Chicago Manual of Style (16^th Edition):

Ekanayaka, Nandula Vidumini. “Growth and Energetics of Cholesterol Utilisation by Mycobacterium smegmatis mc2155 .” 2013. Doctoral Dissertation, University of Otago. Accessed April 15, 2021. http://hdl.handle.net/10523/3743.

MLA Handbook (7^th Edition):

Ekanayaka, Nandula Vidumini. “Growth and Energetics of Cholesterol Utilisation by Mycobacterium smegmatis mc2155 .” 2013. Web. 15 Apr 2021.

Vancouver:

Ekanayaka NV. Growth and Energetics of Cholesterol Utilisation by Mycobacterium smegmatis mc2155 . [Internet] [Doctoral dissertation]. University of Otago; 2013. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10523/3743.

Council of Science Editors:

Ekanayaka NV. Growth and Energetics of Cholesterol Utilisation by Mycobacterium smegmatis mc2155 . [Doctoral Dissertation]. University of Otago; 2013. Available from: http://hdl.handle.net/10523/3743

Dalhousie University

18. Al-Bana, Badii. Characterization of The Viable but Non-Culturable Legionella pneumophila in Water and the Role of 3-Hydroxybutyrate Dehydrogenase in Its Formation.

Degree: PhD, Department of Microbiology & Immunology, 2013, Dalhousie University

URL: http://hdl.handle.net/10222/37024

► Legionella pneumophila, the causative agent of Legionnaires’ disease (LD), is an intracellular pathogen of freshwater protozoa that can also persist in the environment as a… (more)

▼ Legionella pneumophila, the causative agent of Legionnaires’ disease (LD), is an intracellular pathogen of freshwater protozoa that can also persist in the environment as a free-living bacterium. L. pneumophila has many morphological forms that fit within a developmental cycle. In water, L. pneumophila enters into a viable but non-culturable (VBNC) state that is largely uncharacterized. VBNC cells were produced from two developmental L. pneumophila forms, stationary phase forms (SPFs) and mature infectious forms (MIFs) by suspension in double deionized (dd) or tap-water at 45°C. Electron microscopy results showed that VBNC cells have a unique morphology and that in tap water they lose their poly 3-hydroxybutyrate inclusion bodies. Both SPFs and MIFs lost culturability faster in dd- than in tap water, and addition of salts to dd-water prolonged L. pneumophila culturability and enhanced viability. However, MIFs retained higher viability in dd- and tap water (85% and 51%, respectively) than SPFs (5% and 20%, respectively) as determined by the BacLight vital stain. Only ~1 VBNC cell out of 105 of those produced from SPFs in tap water regained culturability via infection of Acanthamoeba. All VBNC cells, except for those produced from SPFs in dd-water, resisted both digestion inside Tetrahymena spp. and detergent-mediated lysis. SDS-PAGE analysis and shotgun proteomics revealed a number of VBNC cell specific proteins; one of these was 3-hydroxybutyrate dehydrogenase (BdhA), which is involved in the metabolism of poly 3-hydroxybutyrate inclusion bodies. A bdhA mutant showed an early loss of culturability and a dramatic decrease in viability as compared to the parent strain, and complementing the mutant with a functional bdhA gene restored the parent's strain phenotypes. In conclusion, VBNC L. pneumophila has a distinct morphology and physiology that varies according to the developmental stage and the environmental conditions used to produce such VBNC cells. VBNC cells have a different protein profile and morphology than the culturable cells, suggesting that this state constitutes a distinct differentiated form within the developmental cycle of L. pneumophila. BdhA seems to influence L. pneumophila survival and hence VBNC cell formation. Collectively, the results from this study provide a better understanding of L. pneumophila VBNC form and the factors influencing its formation. Advisors/Committee Members: Trevor Charles (external-examiner), Brent Johnston (graduate-coordinator), John Rohde, Ross Davidson (thesis-reader), Rafael Garduno, Song Lee (thesis-supervisor), Not Applicable (ethics-approval), Yes (manuscripts), Yes (copyright-release).

Subjects/Keywords: VBNC; water; 3-hydroxybutyrate dehydrogenase; Legionella pneumophila

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APA (6^th Edition):

Al-Bana, B. (2013). Characterization of The Viable but Non-Culturable Legionella pneumophila in Water and the Role of 3-Hydroxybutyrate Dehydrogenase in Its Formation. (Doctoral Dissertation). Dalhousie University. Retrieved from http://hdl.handle.net/10222/37024

Chicago Manual of Style (16^th Edition):

Al-Bana, Badii. “Characterization of The Viable but Non-Culturable Legionella pneumophila in Water and the Role of 3-Hydroxybutyrate Dehydrogenase in Its Formation.” 2013. Doctoral Dissertation, Dalhousie University. Accessed April 15, 2021. http://hdl.handle.net/10222/37024.

MLA Handbook (7^th Edition):

Al-Bana, Badii. “Characterization of The Viable but Non-Culturable Legionella pneumophila in Water and the Role of 3-Hydroxybutyrate Dehydrogenase in Its Formation.” 2013. Web. 15 Apr 2021.

Vancouver:

Al-Bana B. Characterization of The Viable but Non-Culturable Legionella pneumophila in Water and the Role of 3-Hydroxybutyrate Dehydrogenase in Its Formation. [Internet] [Doctoral dissertation]. Dalhousie University; 2013. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10222/37024.

Council of Science Editors:

Al-Bana B. Characterization of The Viable but Non-Culturable Legionella pneumophila in Water and the Role of 3-Hydroxybutyrate Dehydrogenase in Its Formation. [Doctoral Dissertation]. Dalhousie University; 2013. Available from: http://hdl.handle.net/10222/37024

University of Utah

19. Chen, Raymond Feng-Chu. Purification and properties of DPN-linked isocitric dehydrogenases of bovine heart;.

Degree: PhD, Biochemistry;, 1963, University of Utah

URL: http://content.lib.utah.edu/cdm/singleitem/collection/etd1/id/438/rec/1057

► DPN-linked isocitric dehydrogenase has been purified over 700-fold from bovine heart mitochondrial acetone powder. The purified protein exhibits a major component having a sedimentation constant… (more)

▼ DPN-linked isocitric dehydrogenase has been purified over 700-fold from bovine heart mitochondrial acetone powder. The purified protein exhibits a major component having a sedimentation constant of 10.3 S, and the molecular weight has been estimated to be about 3 or 4 x 10 to the fifth power. The turnover number was calculated to be about 8000 moles of DPNH formed per minute per mole of enzyme. ADP has been found to affect this enzyme in several ways. The nucleotide stabilizes the enzyme under conditions of low ionic strength. ADP also enhances the activity of the enzyme, and this effect has been found to be due to a marked diminution of the Km for isocitrate. In addition, Km for metal ions is also reduced by ADP. At low isocitrate concentrations, such as may exist in mitochondria, the enzyme is virtually dependent of ADP for activity. The activating effect of ADP is highly specific since, of a large number of nucleotides tested, only ADP and dADP are stimulatory. In the presence of low concentrations of isocitrate, the pH optimum is displaced from pH 6.7 in the absence of ADP to about pH 7.2 in the absence if ADP leads to similar shift of the pH optimum. The enzyme is inhibited by DPNH, ATP, and ADPR; the inhibition is competitive with DPN+. TPNH potentiates the DPNH inhibition, and both TPNH and DPNH apparently can form fluorimetrically discernible complexes with the enzyme. On the other hand, the TPN-linked isocitric dehydrogenase of bovine heart has been found to be insensitive to DPN+, DPNH, ATP, and ADP. The mechanism of activation by ADP is probably a conformational change in the enzyme which results in the active site become more accessible to substrate. In the ultracentrifuge, it has been shown that the sedimentation velocity of the enzyme is markedly increased by ADP, a finding which suggests that aggregation has occurred. The significance of these finding has been discussed in terms of a possible positive-plus negative feedback control mechanism for mitochondrial oxidation. In addition, stereospecific synthesis of threo-D-isocitrate-?-T and of threo-Ds-isocitrate-?-T have been accomplished enzymically. Oxidation of these compounds by DPN-linked isocitric dehydrogenase revealed that the ?-hydrogen of isocitrate was transferred stereo-specifically and directly to the ?-side of DPN+, and that the ?-hydrogen of isocitrate was retained in ?-ketoglutarate. The ?-hydrogen was also retained during the reaction with TPN-linked isocitric dehydrogenase, thus indicating that the enol form of oxalosuccinate is not likely to occur as a free intermediate in the oxidation of isocitrate. Thus, in all respects, the hydrogen transfer mediated by DPN-linked isocitric dehydrogenase was the same as that catalyzed by the TPN-specific enzyme.

Subjects/Keywords: Dehydrogenase; Isocitrate Concentrations

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APA (6^th Edition):

Chen, R. F. (1963). Purification and properties of DPN-linked isocitric dehydrogenases of bovine heart;. (Doctoral Dissertation). University of Utah. Retrieved from http://content.lib.utah.edu/cdm/singleitem/collection/etd1/id/438/rec/1057

Chicago Manual of Style (16^th Edition):

Chen, Raymond Feng-Chu. “Purification and properties of DPN-linked isocitric dehydrogenases of bovine heart;.” 1963. Doctoral Dissertation, University of Utah. Accessed April 15, 2021. http://content.lib.utah.edu/cdm/singleitem/collection/etd1/id/438/rec/1057.

MLA Handbook (7^th Edition):

Chen, Raymond Feng-Chu. “Purification and properties of DPN-linked isocitric dehydrogenases of bovine heart;.” 1963. Web. 15 Apr 2021.

Vancouver:

Chen RF. Purification and properties of DPN-linked isocitric dehydrogenases of bovine heart;. [Internet] [Doctoral dissertation]. University of Utah; 1963. [cited 2021 Apr 15]. Available from: http://content.lib.utah.edu/cdm/singleitem/collection/etd1/id/438/rec/1057.

Council of Science Editors:

Chen RF. Purification and properties of DPN-linked isocitric dehydrogenases of bovine heart;. [Doctoral Dissertation]. University of Utah; 1963. Available from: http://content.lib.utah.edu/cdm/singleitem/collection/etd1/id/438/rec/1057

Texas A&M University

20. Cheng, Yu-Shan. Mode of Action Study of Para-aminosalicylic Acid and Structure, Function and Inhibitor Study of the Isocitrate Dehydrogenase-2 in Mycobacterium tuberculosis.

Degree: PhD, Chemistry, 2016, Texas A&M University

URL: http://hdl.handle.net/1969.1/187356

► Tuberculosis (TB) killed 1.5 million people and rivaled AIDS, becoming the leading cause of death from infectious disease in 2014. The prevalence of multidrug resistant… (more)

▼ Tuberculosis (TB) killed 1.5 million people and rivaled AIDS, becoming the leading cause of death from infectious disease in 2014. The prevalence of multidrug resistant TB has intensified the current therapeutic procedure, making it urgent to find novel anti-tubercular agents and to come up with solutions to retard the emergence of the drug resistance. This dissertation focuses on the identification of drug targets, the exploration of drug resistance mechanisms, and the identification of novel inhibitors. In the first part, the mechanism of action of the classic anti-tubercular drug, para-aminosalicylic acid (PAS), was explored through genetic, cell viability and molecular modeling studies. Dihydrofolate reductase (DHFR) was identified to be the putative intracellular target of PAS. In addition, the molecular mechanism of PAS resistance was intensively investigated for the clinically relevant Rv2671 up-regulation mutant. Biochemical assays showed that Rv2671 exhibited a low DHFR activity with a high Km for the substrate, 7, 8-dihydrofolate. X-ray crystal structure of the Rv2671 in complex with NADP+ and tetrahydrofolate (THF) further confirmed the structural similarity between Rv2671 and DHFR. These studies together suggested that PAS resistance of this mutant is derived from the ability to complement the DHFR activity with the high level of Rv2671. The second part of this dissertation details the characteristics of Mycobacterium tuberculosis isocitrate dehydrogenase-2 (Mtb IDH2). The kinetic study of Mtb IDH2 suggested that it catalyzes an ordered sequential reaction by binding NADP+ first. X-ray crystal structure revealed the fairly conserved active site and dissimilar overall structure compared to human IDHs (HIDHs), suggesting a potential for drug selectivity. A screening of known inhibitors of mutant HIDHs and a high-throughput screening of Mtb whole cell active compounds were further implemented to identify inhibitors for Mtb IDH2. Two compounds from the screenings exhibited IC50s below 10 μM. The enzyme structure and the modest potency inhibitors of Mtb IDH2 can serve as viable starting points for the follow-up inhibitor development of Mtb IDH2. Advisors/Committee Members: Sacchettini, James C. (advisor), Barondeau, David P. (committee member), Begley, Tadhg (committee member), Straight, Paul (committee member).

Subjects/Keywords: Tuberculosis; isocitrate dehydrogenase; para-aminosalicylic acid; Rv2671

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APA (6^th Edition):

Cheng, Y. (2016). Mode of Action Study of Para-aminosalicylic Acid and Structure, Function and Inhibitor Study of the Isocitrate Dehydrogenase-2 in Mycobacterium tuberculosis. (Doctoral Dissertation). Texas A&M University. Retrieved from http://hdl.handle.net/1969.1/187356

Chicago Manual of Style (16^th Edition):

Cheng, Yu-Shan. “Mode of Action Study of Para-aminosalicylic Acid and Structure, Function and Inhibitor Study of the Isocitrate Dehydrogenase-2 in Mycobacterium tuberculosis.” 2016. Doctoral Dissertation, Texas A&M University. Accessed April 15, 2021. http://hdl.handle.net/1969.1/187356.

MLA Handbook (7^th Edition):

Cheng, Yu-Shan. “Mode of Action Study of Para-aminosalicylic Acid and Structure, Function and Inhibitor Study of the Isocitrate Dehydrogenase-2 in Mycobacterium tuberculosis.” 2016. Web. 15 Apr 2021.

Vancouver:

Cheng Y. Mode of Action Study of Para-aminosalicylic Acid and Structure, Function and Inhibitor Study of the Isocitrate Dehydrogenase-2 in Mycobacterium tuberculosis. [Internet] [Doctoral dissertation]. Texas A&M University; 2016. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/1969.1/187356.

Council of Science Editors:

Cheng Y. Mode of Action Study of Para-aminosalicylic Acid and Structure, Function and Inhibitor Study of the Isocitrate Dehydrogenase-2 in Mycobacterium tuberculosis. [Doctoral Dissertation]. Texas A&M University; 2016. Available from: http://hdl.handle.net/1969.1/187356

Texas A&M University

21. Lalgondar, Mallikarjun. Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH).

Degree: MS, Biochemistry, 2014, Texas A&M University

URL: http://hdl.handle.net/1969.1/152582

► Shikimate dehydrogenase (SDH) is a reversible enzyme catalyzing the reduction of 3-dehydroshikimate (3DHS) to shikimate (SKM) utilizing NADPH cofactor in the shikimate pathway, a central… (more)

▼ Shikimate dehydrogenase (SDH) is a reversible enzyme catalyzing the reduction of 3-dehydroshikimate (3DHS) to shikimate (SKM) utilizing NADPH cofactor in the shikimate pathway, a central route for biosynthesis of aromatic amino acids, folates and ubiquinones in microogransims, plants and parasites, which renders the enzymes of this essential pathway as attractive targets for developing antimicrobials, herbicides and antiparasitic agents. In this study, the crystal structure of Mycobacterium tuberculosis SDH (MtSDH) was determined in the apo-form and in complex with a ligand, SKM. The overall structure of MtSDH contains two structural domains with α/β architecture. The N-terminal substrate binding domain and C-terminal cofactor binding domain are interconnected by two helices forming an active site groove where catalysis occurs. In MtSDH, a series of helices connecting β10 and β11 strands replace a long loop found in other known SDH structures and this region may undergo structural changes upon cofactor binding. NADP^(+) was modeled reliably in the cofactor binding site to gain insight into specific interactions. The analysis reveals that NADP(H) binds in anti conformation and in addition to residues in “basic patch”, Ser125 within the glycine rich loop may interact with the 2'-phosphate of adenine ribose and form a novel cofactor binding microenvironment in SDH family of enzymes. Biochemically, five inhibitors identified previously from a high-throughput enzyme assay screen were evaluated. The IC_(50) values of these compounds range from 2.8-4.6 μM. Further investigation indicates that these compounds display non-competitive or mixed inhibition mode with both substrate and cofactor. This study is expected to provide better understanding of MtSDH structural features and a framework for rational design of inhibitors based on initially characterized compounds. Advisors/Committee Members: Sacchettini, James C (advisor), Barondeau, David P (committee member), Bryk, Mary (committee member).

Subjects/Keywords: Mycobacterium tuberculosis; Shikimate dehydrogenase; Crystal structure; Inhibitors

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APA (6^th Edition):

Lalgondar, M. (2014). Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH). (Masters Thesis). Texas A&M University. Retrieved from http://hdl.handle.net/1969.1/152582

Chicago Manual of Style (16^th Edition):

Lalgondar, Mallikarjun. “Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH).” 2014. Masters Thesis, Texas A&M University. Accessed April 15, 2021. http://hdl.handle.net/1969.1/152582.

MLA Handbook (7^th Edition):

Lalgondar, Mallikarjun. “Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH).” 2014. Web. 15 Apr 2021.

Vancouver:

Lalgondar M. Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH). [Internet] [Masters thesis]. Texas A&M University; 2014. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/1969.1/152582.

Council of Science Editors:

Lalgondar M. Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH). [Masters Thesis]. Texas A&M University; 2014. Available from: http://hdl.handle.net/1969.1/152582

University of Waterloo

22. Asokumar, Navin. Purification and determination of oxidative modifications of the thermostable alcohol dehydrogenase from Thermococcus guaymasensis.

Degree: 2019, University of Waterloo

URL: http://hdl.handle.net/10012/15047

► Hyperthermophiles are microorganisms that grow optimally at 80°C and above. They have been found to be resilient to extremes of pH, redox potential, pressure and… (more)

▼ Hyperthermophiles are microorganisms that grow optimally at 80°C and above. They have been found to be resilient to extremes of pH, redox potential, pressure and salinity. Moreover, they can utilize a wide range of carbohydrates as carbon source and produce ethanol as an end product. Alcohol dehydrogenase (ADH) is a key enzyme responsible for alcohol production, catalyzing interconversions between alcohols and corresponding ketones or aldehydes. ADHs from hyperthermophiles are of great interest due to their thermostability, high activity and enantioselectivity. One such zinc-containing homotetrameric ADH from hyperthermophilic archaeon Thermococcus guaymasensis was found to be 39,395.72 Da per subunit in size, with activity of 1,049 U/mg. Regardless of being a zinc-containing enzyme, this ADH was found to lose its activity when exposed to air. Since zinc is a divalent cation which cannot be further oxidized, a plausible explanation would be that certain amino acids, especially cysteines, succumb to oxidative change, leading to the inactivation of the enzyme under aerobic conditions. TgADH has four Cys residues per subunit; Cys39 (which coordinates with zinc), Cys56, Cys212, and Cys305. The recombinant wild-type (45,260.13 Da per subunit) and Cys mutant TgADH were partially purified from recombinant E. coli host using a heat treatment step, with a specific activity of over 300 U/mg. MALDI-TOF mass spectrometry was used for investigating the modifications due to oxidation in the partially purified recombinant wild-type TgADH, when exposed to air. External calibration resulted in an accuracy range of 0.0013 % - 0.19 %. The higher end of the accuracy range was ≈ 145 times more than the lower end, invalidating the method for the required purpose. However, since 0.0013 % of accuracy was seen for Protein A [M+H]+, which has a mass almost equal to recombinant TgADH, and due to the impure nature of the sample, the method was used for analysis of modifications in the recombinant TgADH, without prior digestion of the enzyme. The measured masses of the active and air-oxidized recombinant TgADH were 47 and 12 Da less than reported mass, respectively. The H2O2-oxidized (1:10, 1:40, 1:160, and 1:400 mol/mol protein subunit:oxidant) TgADH were less than reported masses, whereas they should have been more than the reported mass due to the modification(s). Only the 1:1600 mol/mol H2O2-oxidized sample showed an increase of 360 Da suggesting that Cys residues, along with the Met residues were oxidized. The difference between the measured masses of the active and air-oxidized recombinant TgADH was ≈ 35 Da, which is almost equal to two oxygens. However, due to the large discrepancy in the accuracy range it cannot be conclusively said that two oxygens are being added when the enzyme is exposed to air. Enzyme activity analysis of partially purified C212S and C305S TgADH mutants showed no increase in oxygen tolerance compared to the wild-type TgADH. Since previous studies have eliminated the oxidation of Cys56 being the cause for the loss of…

Subjects/Keywords: hyperthermophile; alcohol dehydrogenase; enzyme purification; Cysteine oxidation

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APA (6^th Edition):

Asokumar, N. (2019). Purification and determination of oxidative modifications of the thermostable alcohol dehydrogenase from Thermococcus guaymasensis. (Thesis). University of Waterloo. Retrieved from http://hdl.handle.net/10012/15047

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Asokumar, Navin. “Purification and determination of oxidative modifications of the thermostable alcohol dehydrogenase from Thermococcus guaymasensis.” 2019. Thesis, University of Waterloo. Accessed April 15, 2021. http://hdl.handle.net/10012/15047.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Asokumar, Navin. “Purification and determination of oxidative modifications of the thermostable alcohol dehydrogenase from Thermococcus guaymasensis.” 2019. Web. 15 Apr 2021.

Vancouver:

Asokumar N. Purification and determination of oxidative modifications of the thermostable alcohol dehydrogenase from Thermococcus guaymasensis. [Internet] [Thesis]. University of Waterloo; 2019. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10012/15047.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Asokumar N. Purification and determination of oxidative modifications of the thermostable alcohol dehydrogenase from Thermococcus guaymasensis. [Thesis]. University of Waterloo; 2019. Available from: http://hdl.handle.net/10012/15047

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Penn State University

23. Radle, Matt. Investigation of Formate Dehyrogenase and Sulfite Reductase Variants as Candidates for A Photosystem I Nanoconstruct.

Degree: 2015, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/26501

► A novel method of light-driven hydrogen production in which photosystem I (PSI) acts as a photosensitizer and transports electrons to a tethered [FeFe] hydrogenase was… (more)

Subjects/Keywords: photosystem I; formate dehydrogenase; sulfite reductase

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APA (6^th Edition):

Radle, M. (2015). Investigation of Formate Dehyrogenase and Sulfite Reductase Variants as Candidates for A Photosystem I Nanoconstruct. (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/26501

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Radle, Matt. “Investigation of Formate Dehyrogenase and Sulfite Reductase Variants as Candidates for A Photosystem I Nanoconstruct.” 2015. Thesis, Penn State University. Accessed April 15, 2021. https://submit-etda.libraries.psu.edu/catalog/26501.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Radle, Matt. “Investigation of Formate Dehyrogenase and Sulfite Reductase Variants as Candidates for A Photosystem I Nanoconstruct.” 2015. Web. 15 Apr 2021.

Vancouver:

Radle M. Investigation of Formate Dehyrogenase and Sulfite Reductase Variants as Candidates for A Photosystem I Nanoconstruct. [Internet] [Thesis]. Penn State University; 2015. [cited 2021 Apr 15]. Available from: https://submit-etda.libraries.psu.edu/catalog/26501.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Radle M. Investigation of Formate Dehyrogenase and Sulfite Reductase Variants as Candidates for A Photosystem I Nanoconstruct. [Thesis]. Penn State University; 2015. Available from: https://submit-etda.libraries.psu.edu/catalog/26501

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

24. Thanya Sripo. Cloning, sequencing and expression of aldehyde dehydrogenase gene from Halomonas salina AS11 .

Degree: คณะวิทยาศาสตร์ ภาควิชาชีวเคมี, 2001, Prince of Songkla University

URL: http://kb.psu.ac.th/psukb/handle/2016/10875

Subjects/Keywords: Aldehyde dehydrogenase; Dehydrogenases

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APA (6^th Edition):

Sripo, T. (2001). Cloning, sequencing and expression of aldehyde dehydrogenase gene from Halomonas salina AS11 . (Thesis). Prince of Songkla University. Retrieved from http://kb.psu.ac.th/psukb/handle/2016/10875

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Sripo, Thanya. “Cloning, sequencing and expression of aldehyde dehydrogenase gene from Halomonas salina AS11 .” 2001. Thesis, Prince of Songkla University. Accessed April 15, 2021. http://kb.psu.ac.th/psukb/handle/2016/10875.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Sripo, Thanya. “Cloning, sequencing and expression of aldehyde dehydrogenase gene from Halomonas salina AS11 .” 2001. Web. 15 Apr 2021.

Vancouver:

Sripo T. Cloning, sequencing and expression of aldehyde dehydrogenase gene from Halomonas salina AS11 . [Internet] [Thesis]. Prince of Songkla University; 2001. [cited 2021 Apr 15]. Available from: http://kb.psu.ac.th/psukb/handle/2016/10875.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Sripo T. Cloning, sequencing and expression of aldehyde dehydrogenase gene from Halomonas salina AS11 . [Thesis]. Prince of Songkla University; 2001. Available from: http://kb.psu.ac.th/psukb/handle/2016/10875

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Guelph

25. Carere, Jason. An Investigation of the Molecular Determinants of Substrate Channeling and Allosteric Activation in Aldolase-Dehydrogenase Complexes.

Degree: PhD, Department of Molecular and Cellular Biology, 2013, University of Guelph

URL: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/6623

► The aldolase-dehydrogenase complex catalyzes the last two steps in the microbial meta-cleavage pathway of various aromatic compounds including polychlorinated biphenyls (bph pathway) and cholesterol (hsa… (more)

▼ The aldolase-dehydrogenase complex catalyzes the last two steps in the microbial meta-cleavage pathway of various aromatic compounds including polychlorinated biphenyls (bph pathway) and cholesterol (hsa pathway). The aldolase, BphI, cleaves 4-hydroxy-2-oxoacids to produce pyruvate and an aldehyde. Linear aldehydes of up to six carbons long and branched isobutyraldehyde were directly channeled to the aldehyde dehydrogenase BphJ, via a molecular tunnel, with greater than 80% efficiency. The molecular tunnel is narrow in positions lined by Gly-322 and Gly-323 in the aldolase. BphI variants G322F, G322L and G323F were found to block aldehyde channeling. The replacement of Asn-170 in BphJ with alanine and aspartate did not substantially alter aldehyde channeling efficiencies, thus disproving a previous hypothesis that hydrogen bonding between the Asn-170 and the nicotinamide cofactor induces the opening of the exit of the tunnel. The H20A and Y290F BphI variants displayed significantly reduced aldehyde channeling efficiencies indicating that these residues control the entry and exit of substrates and products from the aldolase reaction. The BphI reaction was activated by NADH binding to BphJ in the wild-type enzyme and channel blocked variants. Activation of BphI by BphJ N170A, N170D and I171A was decreased by ≥ 3-fold in the presence of NADH and ≥ 4.5-fold when BphJ was undergoing turnover. These results demonstrate that the dehydrogenase coordinates catalytic activity of BphI through allostery rather than through faster aldehyde release from substrate channeling. HsaF, an ortholog of BphI from Mycobacterium tuberculosis could be expressed as a soluble dimer, however HsaF was inactive in the absence of HsaG, a BphJ ortholog. Acetaldehyde and propionaldehyde were channeled directly to HsaG with similar efficiencies as in the BphI-BphJ system. The HsaF-HsaG complex was crystallized and its structure solved to a resolution of 1.93 Å. Substitution of Ser-41 in HsaG with isoleucine or aspartate resulted in about 35-fold increase in Km for CoA but only 4-fold increase in Km for dephospho-CoA, confirming its importance in interacting with the 3’- ribose phosphate of CoA. A second gene annotated as 4-hydroxy-2-oxopentanoic acid aldolase (Rv3469c) from M. tuberculosis was expressed, purified and found to possess oxaloacetate decarboxylase and not aldolase activity. Advisors/Committee Members: Seah, Stephen (advisor).

Subjects/Keywords: Aldolase; Dehydrogenase; Channeling; Crystallography; Allostery; Cholesterol; PCBs

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APA (6^th Edition):

Carere, J. (2013). An Investigation of the Molecular Determinants of Substrate Channeling and Allosteric Activation in Aldolase-Dehydrogenase Complexes. (Doctoral Dissertation). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/6623

Chicago Manual of Style (16^th Edition):

Carere, Jason. “An Investigation of the Molecular Determinants of Substrate Channeling and Allosteric Activation in Aldolase-Dehydrogenase Complexes.” 2013. Doctoral Dissertation, University of Guelph. Accessed April 15, 2021. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/6623.

MLA Handbook (7^th Edition):

Carere, Jason. “An Investigation of the Molecular Determinants of Substrate Channeling and Allosteric Activation in Aldolase-Dehydrogenase Complexes.” 2013. Web. 15 Apr 2021.

Vancouver:

Carere J. An Investigation of the Molecular Determinants of Substrate Channeling and Allosteric Activation in Aldolase-Dehydrogenase Complexes. [Internet] [Doctoral dissertation]. University of Guelph; 2013. [cited 2021 Apr 15]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/6623.

Council of Science Editors:

Carere J. An Investigation of the Molecular Determinants of Substrate Channeling and Allosteric Activation in Aldolase-Dehydrogenase Complexes. [Doctoral Dissertation]. University of Guelph; 2013. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/6623

University of KwaZulu-Natal

26. Eugene, Katapazi. Recombinant expression and bioinformatic analysis of plasmodium falciparum lactate dehydrogenase and heat shock protein 70-1.

Degree: 2017, University of KwaZulu-Natal

URL: http://hdl.handle.net/10413/16076

► Malaria remains a serious human health problem and the disease is particularly prevalent in developing countries. Malaria is caused by a parasite of the genus… (more)

▼ Malaria remains a serious human health problem and the disease is particularly prevalent in developing countries. Malaria is caused by a parasite of the genus Plasmodium. Diagnosis of malaria is required before any treatment or intervention. The gold standard for malaria diagnosis is microscopy. Rapid diagnostic tests (RDT) have been used at point-of-care because of their relative ease of use. Correct and accurate diagnosis of malaria is a prerequisite as a point-of-care intervention aimed at eradication, detection of an asymptomatic reservoir, quantification of parasite load and tracking of drug resistance to malaria. Therefore, RDTs that have high sensitivity and specificity are required. Plasmodium LDH (PLDH) is one of the three proteins in current use as antibody targets in RDTs to detect human malaria. The other two proteins are Plasmodium falciparum histidine rich protein II (PfHRPII) and aldolase. Of the three proteins, HRPII is the most widely used protein in RDTs in sub-Saharan Africa. One of the requirements in improving the current RDTs is to improve specificity and sensitivity. Plasmodium falciparum heat shock protein 70-1 (PfHSP70-1) has been found to be immunogenic in infected humans, abundantly expressed in the asexual stages and thought to be a potential diagnostic target for malaria. Conditions were optimized for the recombinant expression of PfLDH and PfHSP70-1 in different growth media, temperatures, concentrations of IPTG, times of induction, stages at which IPTG is introduced, use of a single colony as starting material or a dilution of an overnight culture to inoculate fresh media. Terrific Broth was found to be a better growth medium than Lysogeny Broth and does not require induction with IPTG. Use of a single starting colony was found to be better than dilution of an overnight culture as it saves time. Inducing at the stationary phase of bacterial growth yields more soluble protein than at mid-log phase. Expressing at lower temperatures lower than 37°C produces more soluble protein than growth at 37°C. Methods of lysing the host bacterial cells expressing PfLDH and PfHSP70-1 by freezing and thawing, sonication, lysozyme digestion and a combination of these methods were compared and optimized. The combination of freeze and thaw followed by repeated sonication was found to be optimal for lysing the E. coli host cells. Both proteins were affinity purified using an affinity Talon® resin and proteins were eluted with 150 mM imidazole. The purification protocol was monitored by separating the proteins on a 12.5% sodium dodecyl sulphate polyacrylamide electrophoresis gel. Purifying recombinant protein at 4°C produced higher yields of recombinant protein. The identity of the recombinant protein was confirmed by probing a western blot with anti-His-tag antibodies against each protein. The anti-His-tag antibodies detected both PfLDH and PfHSP70-1. Preliminary experiments on PfLDH enzyme found that the recombinant enzyme was active. In silico studies were done on PfLDH and PfHSP70-1 to identify… Advisors/Committee Members: Goldring, Dean J. P. (advisor).

Subjects/Keywords: Plasmodium.; Falciparum.; Lactate dehydrogenase.; Malakia.; HSP70.

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APA (6^th Edition):

Eugene, K. (2017). Recombinant expression and bioinformatic analysis of plasmodium falciparum lactate dehydrogenase and heat shock protein 70-1. (Thesis). University of KwaZulu-Natal. Retrieved from http://hdl.handle.net/10413/16076

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Eugene, Katapazi. “Recombinant expression and bioinformatic analysis of plasmodium falciparum lactate dehydrogenase and heat shock protein 70-1.” 2017. Thesis, University of KwaZulu-Natal. Accessed April 15, 2021. http://hdl.handle.net/10413/16076.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Eugene, Katapazi. “Recombinant expression and bioinformatic analysis of plasmodium falciparum lactate dehydrogenase and heat shock protein 70-1.” 2017. Web. 15 Apr 2021.

Vancouver:

Eugene K. Recombinant expression and bioinformatic analysis of plasmodium falciparum lactate dehydrogenase and heat shock protein 70-1. [Internet] [Thesis]. University of KwaZulu-Natal; 2017. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10413/16076.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Eugene K. Recombinant expression and bioinformatic analysis of plasmodium falciparum lactate dehydrogenase and heat shock protein 70-1. [Thesis]. University of KwaZulu-Natal; 2017. Available from: http://hdl.handle.net/10413/16076

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Universidade Nova

27. Fonseca, Luís Filipe Madureira. Bioremediation and CO2 scavenging using molybdenum-containing enzymes.

Degree: 2015, Universidade Nova

URL: http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/14581

► Carbon dioxide valorization, will not only help to relieve the greenhouse effect but might also allow us to transform it in value-added chemicals that will… (more)

▼ Carbon dioxide valorization, will not only help to relieve the greenhouse effect but might also allow us to transform it in value-added chemicals that will help overcoming the energy crisis. To accomplish this goal, more research that focus on sequestering CO2 and endeavors through a carbon-neutral or carbon-negative strategy is needed in order to handle with the dwindling fossil fuel supplies and their environmental impact. Formate dehydrogenases are a promising means of turning CO2 into a biofuel that will allow for a reduction of greenhouse gas emissions and for a significant change to the economic paramount. The main objective of this work was to assess whether a NAD+-independent molybdenum-containing formate dehydrogenase is able to catalyze the reduction of CO2 to formate. To achieve this, a molybdenum-containing formate dehydrogenase was isolated from the sulfate reducing bacteria Desulfovibrio desulfuricans ATCC 27774. Growth conditions were found that allowed for a greater cellular mass recovery and formate dehydrogenase expression. After growth trials, kinetic assays for formate oxidation and CO2 reduction were performed and kinetic parameters determined. For the formate oxidation reaction, a KM of 49 μM and a turnover constant of 146 s-1 were determined. These kinetic parameters are in agreement with those determined by Mota, et al. (2011). Finally, we found that this molybdenum-containing enzyme was able to catalyze the reduction of CO2 to formate with a turnover constant of 4.6 s-1 and a KM of 13 μM. For the first time a NAD+-independent molybdenum-containing formate dehydrogenase was found to catalyze CO2 reduction, allowing its use as a biocatalyst in energetically efficient CO2 fixation processes that can be directed towards bioremediation or as an alternative and renewable energy source. Characterizing these enzymes may lead to the development of more efficient synthetic catalysts, make them readily available and more suited for practical applications. Advisors/Committee Members: Moura, José, Moura, Isabel, Maia, Luísa.

Subjects/Keywords: Formate dehydrogenase; Molybdoenzymes; CO2 reduction; Bioremediation

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Fonseca, L. F. M. (2015). Bioremediation and CO2 scavenging using molybdenum-containing enzymes. (Thesis). Universidade Nova. Retrieved from http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/14581

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Fonseca, Luís Filipe Madureira. “Bioremediation and CO2 scavenging using molybdenum-containing enzymes.” 2015. Thesis, Universidade Nova. Accessed April 15, 2021. http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/14581.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Fonseca, Luís Filipe Madureira. “Bioremediation and CO2 scavenging using molybdenum-containing enzymes.” 2015. Web. 15 Apr 2021.

Vancouver:

Fonseca LFM. Bioremediation and CO2 scavenging using molybdenum-containing enzymes. [Internet] [Thesis]. Universidade Nova; 2015. [cited 2021 Apr 15]. Available from: http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/14581.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Fonseca LFM. Bioremediation and CO2 scavenging using molybdenum-containing enzymes. [Thesis]. Universidade Nova; 2015. Available from: http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/14581

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Vienna

28. Ruppert, Josef. Enzymkinetische Untersuchungen cyanobakterieller Succinatdehydrogenase in getrennten und gereinigten Membranen von Synechocystis (PCC 6803) und Synechococcus (PCC 6301).

Degree: 2010, University of Vienna

URL: http://othes.univie.ac.at/12040/

► Diese Untersuchung des für die Atmung essentiellen Enzyms Succinatdehydrogenase wurde an beiden Membransystemen von zwei Cyanobakterien-Spezies durchgeführt da hier die atmungsaktiven Membranen nicht durch Kompartimentierung… (more)

Subjects/Keywords: 42.20 Genetik; Cyanobakterien / Respiration / Succinat-Dehydrogenase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Ruppert, J. (2010). Enzymkinetische Untersuchungen cyanobakterieller Succinatdehydrogenase in getrennten und gereinigten Membranen von Synechocystis (PCC 6803) und Synechococcus (PCC 6301). (Thesis). University of Vienna. Retrieved from http://othes.univie.ac.at/12040/

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Ruppert, Josef. “Enzymkinetische Untersuchungen cyanobakterieller Succinatdehydrogenase in getrennten und gereinigten Membranen von Synechocystis (PCC 6803) und Synechococcus (PCC 6301).” 2010. Thesis, University of Vienna. Accessed April 15, 2021. http://othes.univie.ac.at/12040/.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Ruppert, Josef. “Enzymkinetische Untersuchungen cyanobakterieller Succinatdehydrogenase in getrennten und gereinigten Membranen von Synechocystis (PCC 6803) und Synechococcus (PCC 6301).” 2010. Web. 15 Apr 2021.

Vancouver:

Ruppert J. Enzymkinetische Untersuchungen cyanobakterieller Succinatdehydrogenase in getrennten und gereinigten Membranen von Synechocystis (PCC 6803) und Synechococcus (PCC 6301). [Internet] [Thesis]. University of Vienna; 2010. [cited 2021 Apr 15]. Available from: http://othes.univie.ac.at/12040/.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Ruppert J. Enzymkinetische Untersuchungen cyanobakterieller Succinatdehydrogenase in getrennten und gereinigten Membranen von Synechocystis (PCC 6803) und Synechococcus (PCC 6301). [Thesis]. University of Vienna; 2010. Available from: http://othes.univie.ac.at/12040/

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Cambridge

29. Casey, Ruth. A study of succinate dehydrogenase deficient tumourigenesis: From functional assessment of variant pathogenicity to the discovery of new disease biomarkers.

Degree: PhD, 2019, University of Cambridge

URL: https://www.repository.cam.ac.uk/handle/1810/291871

► A loss of function of the citric acid cycle enzyme complex succinate dehydrogenase (SDH) is associated with a predisposition to a spectrum of tumourigenesis including… (more)

Subjects/Keywords: Phaeochromocytoma; paraganglioma; Succinate dehydrogenase; metabolomics; GIST

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Casey, R. (2019). A study of succinate dehydrogenase deficient tumourigenesis: From functional assessment of variant pathogenicity to the discovery of new disease biomarkers. (Doctoral Dissertation). University of Cambridge. Retrieved from https://www.repository.cam.ac.uk/handle/1810/291871

Chicago Manual of Style (16^th Edition):

Casey, Ruth. “A study of succinate dehydrogenase deficient tumourigenesis: From functional assessment of variant pathogenicity to the discovery of new disease biomarkers.” 2019. Doctoral Dissertation, University of Cambridge. Accessed April 15, 2021. https://www.repository.cam.ac.uk/handle/1810/291871.

MLA Handbook (7^th Edition):

Casey, Ruth. “A study of succinate dehydrogenase deficient tumourigenesis: From functional assessment of variant pathogenicity to the discovery of new disease biomarkers.” 2019. Web. 15 Apr 2021.

Vancouver:

Casey R. A study of succinate dehydrogenase deficient tumourigenesis: From functional assessment of variant pathogenicity to the discovery of new disease biomarkers. [Internet] [Doctoral dissertation]. University of Cambridge; 2019. [cited 2021 Apr 15]. Available from: https://www.repository.cam.ac.uk/handle/1810/291871.

Council of Science Editors:

Casey R. A study of succinate dehydrogenase deficient tumourigenesis: From functional assessment of variant pathogenicity to the discovery of new disease biomarkers. [Doctoral Dissertation]. University of Cambridge; 2019. Available from: https://www.repository.cam.ac.uk/handle/1810/291871

Université Catholique de Louvain

30. Khan, Mohammad Shahneawz. In vivo promiscuity and directed evolution of oligomeric beta-decarboxylating dehydrogenases.

Degree: 2018, Université Catholique de Louvain

URL: http://hdl.handle.net/2078.1/202599

►

At the molecular level, natural evolution gave rise a wide variety of proteins endowed with exquisite properties. In this study, we envisioned to contribute a… (more)

▼

At the molecular level, natural evolution gave rise a wide variety of proteins endowed with exquisite properties. In this study, we envisioned to contribute a better understanding of the evolutionary mechanisms and structure function relationships of oligomeric enzymes. Beta-decarboxylating dehydrogenases were chosen as a model superfamily. Oligomerization is an advantage for complexifying the properties of a protein such as affording allosterism; however, the impact of oligomerization on the evolutionary mechanisms of proteins is poorly documented. This study will explore the potential of β-decarboxylating dehydrogenases as a platform for directed evolution of oligomeric enzymes using a strategy of activity interconversion between the family members. We first studied the promiscuous activities of D-malate and 3-isopropylmalate dehydrogenases (DmlA and IPMDH) in vivo and showed reciprocal complementation of each enzyme in Escherichia coli strains where the other enzyme is absent. By simulating gene duplication, we demonstrated that heteromeric complex of DmlA is formed in vivo from the interaction of the subunits encoded from the two copies of the gene. Following a directed evolution approach, we successfully generated a NAD dependent E. coli isocitrate dehydrogenase (IDH) from DmlA. We found that a single amino acid substitution (Leu89Ser) endows DmlA with about 60000-fold improvement in IDH activity although the IDH phenotype in vivo is thermosensitive. Co-expression of the wild type DmlA enzyme with the mutant did not result in an increased thermostability indicating that, in this specific case of molecular evolution, there is no paralogous chaperoning from the parental protein in the oligomeric assembly.

(SC - Sciences) – UCL, 2018

Advisors/Committee Members: UCL - SST / LIBST - Louvain Institute of Biomolecular Science and Technology, UCL - Faculty of Sciences, Boutry, Marc, Batoko, Henri, Hollfelder, Florian, Joris, Bernard, Hallet, Bernard, Soumillion, Patrice.

Subjects/Keywords: Enzyme; Promiscuity; Directed Evolution; Beta-decarboxylating dehydrogenase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Khan, M. S. (2018). In vivo promiscuity and directed evolution of oligomeric beta-decarboxylating dehydrogenases. (Thesis). Université Catholique de Louvain. Retrieved from http://hdl.handle.net/2078.1/202599

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Khan, Mohammad Shahneawz. “In vivo promiscuity and directed evolution of oligomeric beta-decarboxylating dehydrogenases.” 2018. Thesis, Université Catholique de Louvain. Accessed April 15, 2021. http://hdl.handle.net/2078.1/202599.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Khan, Mohammad Shahneawz. “In vivo promiscuity and directed evolution of oligomeric beta-decarboxylating dehydrogenases.” 2018. Web. 15 Apr 2021.

Vancouver:

Khan MS. In vivo promiscuity and directed evolution of oligomeric beta-decarboxylating dehydrogenases. [Internet] [Thesis]. Université Catholique de Louvain; 2018. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/2078.1/202599.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Khan MS. In vivo promiscuity and directed evolution of oligomeric beta-decarboxylating dehydrogenases. [Thesis]. Université Catholique de Louvain; 2018. Available from: http://hdl.handle.net/2078.1/202599

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

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