Relevant bibliographies by topics / Mercaptopyruvate sulfurtransferase

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  2. Dissertations / Theses
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Academic literature on the topic 'Mercaptopyruvate sulfurtransferase'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "Mercaptopyruvate sulfurtransferase"

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Nagahara, Noriyuki. "Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System." Biomolecules 10, no. 6 (May 28, 2020): 826. http://dx.doi.org/10.3390/biom10060826.

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Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant Escherichia coli glutaredoxin1 (Cys14 is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.
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Nagahara, Noriyuki. "Catalytic Site Cysteines of Thiol Enzyme: Sulfurtransferases." Journal of Amino Acids 2011 (December 28, 2011): 1–7. http://dx.doi.org/10.4061/2011/709404.

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Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active. Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a thiol or a thiolate. The redox changes of these enzymes are involved in their catalytic processes. On the other hand, transferases, and also some phosphatases and hydrolases, have a single-catalytic site cysteine residue. The cysteines are redox active, but their sulfenyl forms, which are inactive, are not well explained biologically. In particular, oxidized forms of sulfurtransferases, such as mercaptopyruvate sulfurtransferase and thiosulfate sulfurtransferase, are not reduced by reduced glutathione but by reduced thioredoxin. This paper focuses on why the catalytic site cysteine of sulfurtransferase is redox active.
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Porter, Dale W., and Steven I. Baskin. "Specificity studies of 3-mercaptopyruvate sulfurtransferase." Journal of Biochemical Toxicology 10, no. 6 (October 1995): 287–92. http://dx.doi.org/10.1002/jbt.2570100602.

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Mitidieri, Emma, Teresa Tramontano, Danila Gurgone, Valentina Citi, Vincenzo Calderone, Vincenzo Brancaleone, Antonia Katsouda, et al. "Mercaptopyruvate acts as endogenous vasodilator independently of 3-mercaptopyruvate sulfurtransferase activity." Nitric Oxide 75 (May 2018): 53–59. http://dx.doi.org/10.1016/j.niox.2018.02.003.

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Nagahara, Noriyuki. "S9-2 Mercaptopyruvate sulfurtransferase and hydrogen sulfide." Nitric Oxide 39 (May 2014): S12. http://dx.doi.org/10.1016/j.niox.2014.03.044.

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Alphey, Magnus S., Roderick A. M. Williams, Jeremy C. Mottram, Graham H. Coombs, and William N. Hunter. "The Crystal Structure ofLeishmania major3-Mercaptopyruvate Sulfurtransferase." Journal of Biological Chemistry 278, no. 48 (September 1, 2003): 48219–27. http://dx.doi.org/10.1074/jbc.m307187200.

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Nagahara, Noriyuki, Taro Yoshii, Yasuko Abe, and Tomohiro Matsumura. "Thioredoxin-dependent Enzymatic Activation of Mercaptopyruvate Sulfurtransferase." Journal of Biological Chemistry 282, no. 3 (November 27, 2006): 1561–69. http://dx.doi.org/10.1074/jbc.m605931200.

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Tomita, Masahiro, Noriyuki Nagahara, and Takaaki Ito. "Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse." Molecules 21, no. 12 (December 11, 2016): 1707. http://dx.doi.org/10.3390/molecules21121707.

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Peleli, Maria, Sofia-Iris Bibli, Zhen Li, Athanasia Chatzianastasiou, Aimilia Varela, Antonia Katsouda, Sven Zukunft, et al. "Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase." Biochemical Pharmacology 176 (June 2020): 113833. http://dx.doi.org/10.1016/j.bcp.2020.113833.

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Katsouda, Antonia, Nikos Malissovas, Andreas Papapetropoulos, and Dimitris Beis. "Function of 3-mercaptopyruvate sulfurtransferase in zebrafish (Danio rerio)." Nitric Oxide 47 (May 2015): S38. http://dx.doi.org/10.1016/j.niox.2015.02.092.

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Dissertations / Theses on the topic "Mercaptopyruvate sulfurtransferase"

1

Jutabha, Promjit. "Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli." Diss., Virginia Tech, 2001. http://hdl.handle.net/10919/28109.

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Sulfurtransferases, including mercaptopyruvate sulfurtransferase and rhodanese, are widely distributed in living organisms. Mercaptopyruvate sulfurtransferase and rhodanese catalyze the transfer of sulfur from mercaptopyruvate and thiosulfate, respectively, to sulfur acceptors such as thiols or cyanide. There is evidence to suggest that rhodanese can mobilize sulfur from thiosulfate for in vitro formation of iron-sulfur clusters. Additionally, primary sequence analysis reveals that MoeB from some organisms, as well as ThiI of Escherichia coli, contain a C-terminal sulfurtransferase domain. MoeB is required for molybdopterin biosynthesis, whereas ThiI is necessary for biosynthesis of thiamin and 4-thiouridine in transfer ribonucleic acid. These observations led to the hypothesis that sulfurtransferases might be involved in sulfur transfer for biosynthesis of some sulfur-containing cofactors (e.g., biotin, lipoic acid, thiamin and molybdopterin). Results of a BLAST search revealed that E. coli has at least eight potential sulfurtransferases, besides ThiI. Previously, a glpE-encoded rhodanese of E. coli was characterized in our laboratory. In this dissertation, a mercaptopyruvate sulfurtransferase and corresponding gene (sseA) of E. coli were identified. In addition, the possibility that mercaptopyruvate sulfurtransferase could participate or work in concert with a cysteine desulfurase, IscS, in the biosynthesis of cofactors was examined. Cloning of the sseA gene and biochemical characterization of the corresponding protein were used to show that SseA is a mercaptopyruvate sulfurtransferase of E. coli. A strain with a chromosomal insertion mutation in sseA was constructed in order to characterize the physiological function of mercaptopyruvate sulfurtransferase. However, the lack of SseA did not result in a discernable phenotypic change. Redundancy of sulfurtransferases in E. coli may prevent the appearance of a phenotypic change due to the loss of a single sulfurtransferase. Subsequently, other paralogous genes for putative sulfurtransferases, including ynjE and yceA, were cloned. Strains with individual deletions of the chromosomal ynjE and yceA genes were also constructed. Finally, strains with multiple deficiency in potential sulfurtransferase genes, including sseA, ynjE and glpE, as well as iscS, were created. However, no phenotype associated with combinations of sseA, glpE and/or ynjE deficiency was identified. Therefore, the physiological functions of mercaptopyruvate sulfurtransferase and related sulfurtransferases remain unknown.
Ph. D.
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2

Williams, Roderick Adeyinka Malcolm. "Mercaptopyruvate sulfurtransferase and cysteine biosynthetic pathways in Leishmania." Thesis, University of Glasgow, 2003. http://theses.gla.ac.uk/8317/.

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Coping with oxidative stress is vital for survival of the intracellular parasite Leishmania, but the complex biochemical mechanisms involved are not fully understood. This study focused on enzymes of cysteine metabolism in Leishmania and the parts they play. Mercaptopyruvate sulfurtransferase (EC 2.8.1.2) of Leishmania major and L. mexicana and serine acetyltransferase (EC 2.1.3.30), cysteine synthase (EC 4.2.99.8) and cystathionine b-synthase (EC 4.2.1.22) of Leishmania major have been cloned, expressed as active enzymes in Escherichia coli, and characterised. The leishmanial mercaptopyruvate sulfurtransferase is structurally peculiar in possessing a C-terminal domain of some 70 amino acids. Homologous genes of T. cruzi and T. brucei encode enzymes with a similar C-terminal domain, which suggests that the feature, not known in any other sulfurtranferase, is a characteristic of trypanosomatid parasites. Short truncations of the C-terminal domain resulted in misfolded, inactive proteins, demonstrating that the domain plays some key role in facilitating correct folding of the enzymes. The recombinant sulfurtransferase exhibit high activity towards 3-mercaptopyruvate and catalyse the transfer of sulfane to cyanide to form thiocyanate and sulfide. The sulfide can react with O-acetyl serine to yield cysteine through the action of cysteine synthase. They also use thiosulfate as a substrate and mercaptoethanol, glutathione, cysteine or reduced thioredoxin as the accepting nucleophile, the latter being oxidised. Mercaptopyruvate sulfurtransferase and cysteine synthase are expressed in all life cycle stages of Leishmania and the expression levels are increased under hypo-sulfur stress. The expression level of mercaptopyruvate sulfurtransferase is also increased under oxidative stress whereas overexpression of serine acetyltransferase, cysteine synthase and cystathionine beta-synthase in Leishmania promastigotes produced cell lines resistant to the oxidants hydrogen peroxide (0.5 mM), tert-butyl hydroperoxide (10 mM) and cumene hydroperoxide (10 mM).
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Billaut-Laden, Ingrid. "Etude du polymorphisme génétique de la mercaptopyruvate sulfurtransférase (MPST) et de la thiosulfate sulfurtransférase (TST ou rhodanèse), enzymes impliquées dans la détoxication des cyanures chez l'homme." Lille 2, 2006. http://www.theses.fr/2006LIL2S014.

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La Mercaptopyruvate Sulfurtransférase (MPST) et la Thiosulfate Sulfurtransférase (TST) sont deux enzymes jouant un rôle central dans la détoxification des cyanures. Un défaut d'activité, d'origine génétique, de ces enzymes pourrait être à l'origine de variations interindividuelles de susceptibilité à la toxicité des cyanures et être impliqué dans la genèse et/ou l'évolution de maladies héréditaires. Notre travail a consisté à évaluer la nature et l'étendue de la variabilité de la séquence nucléotidique des gènes de ces deux enzymes dans une population d'individus sains et de patients atteints de deux pathologies intestinales à composante environnementale et génétique, à l'aide d'une stratégie basée sur le couplage de l'analyse du polymorphisme de conformation de fragments d'ADN simple brin générés par réaction de polymérisation en chaîne (PCR-SSCP) et du séquençage. Ce travail nous a permis d'identifier de nombreux variants de ces gènes. L'étude in vitro et in vivo des conséquences fonctionnelles de ces variants sur l'expression des gènes et l'activité des enzymes codées a ensuite été effectuée. Les résultats de ce travail démontrent pour la première fois l'existence d'un polymorphisme génétique fonctionnel de la MPST et de la TST. Les conséquences cliniques de ces polymorphismes restent à démonter
The Mercaptopyruvate Sulfurtransférase (MPST) and the Thiosulfate Sulfurtransférase (TST) are both key enzymes in cyanide detoxification. A deficiency of genetic origin in MPST or TST activity would lead to interindividual variability in susceptibility to cyanide and, consequently, could be involved in the pathogenesis of environmental diseases (ulcerative colitis and Crohn disease). The present work consisted first in the mutational screening of the MPST and TST genes in DNA samples from large groups of healthy individuals and patients, using a PCR-SSCP strategy and sequencing. This strategy allowed us to identify numerous polymorphisms in both genes. The functional consequences of some of the identified polymorphisms were then assessed by in vitro and in vivo assays. Our findings revealed for the first time the existence of a functional genetic polymorphism of MPST and TST. The clinical relevance of these genetic polymorphisms remains to be analysed
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Chen, Ying-Siao, and 陳盈孝. "Theoretical study on the dethiolation mechanism of human 3-mercaptopyruvate sulfurtransferase." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/268vsr.

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碩士
國立交通大學
生物科技系所
103
The human mercaptopyruvate sulfurtransferase (h-MST) is able to alleviate the physiological cyanide poisoning, and the detoxification process involves the formation of persulfide bond followed by dethiolation. At the stage of persulfide formation, the sulfur atom transfers from the 3-mercaptopyruvate (3-MP) to the Cys248 residue of the h-MST and produces the persulfidated Cys248 residue and pyruvate. In this study we aim at the mechanisms of the dethiolation process, and firstly construct the CG model to perform the simulation. The CG model that consists of cysteine-glycine dipeptide and cyanide (CN-) is preliminarily constructed to optimize the geometry, and to depict the potential energy surfaces (PES) using density functional theories (DFT) as well as the second order Møller-Plesset perturbation theory (MP2). In this model, cyanide reacts with the aforementioned persulfidated Cys248 residue and finally produces the less toxic thiocyanate (SCN-) via a two-step mechanism: the first step is the persulfide bond cleavage, while the second step involves the proton transfer. The energy barriers of the two steps are 55.5 kcal/mol and 40.1 kcal/mol at the level of B3LYP/6-311++G(d,p), while MP2 theory gives higher values at 55.0 kcal/mol and 45.7 kcal/mol using triple-zeta 6-311++G(d,p) basis set. In addition, the reaction is further investigated in the protein system (PDB code: 4JGT) utilizing a two-layer ONIOM scheme, and the simulations suggest a concerted route with only one transition state. At ONIOM(B3LYP:AMBER) level, the activation energy is computed at 45.6 kcal/mol, and the activation barrier is elevated to 58.4 kcal/mol at ONIOM(MP2:AMBER) level. In conclusion, the high activation barrier in both of the CG model and the protein system might explain the fatality of cyanide poisoning though the existence of MSTs in vivo.
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Book chapters on the topic "Mercaptopyruvate sulfurtransferase"

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Schomburg, Dietmar, and Dörte Stephan. "3-Mercaptopyruvate sulfurtransferase." In Enzyme Handbook, 891–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_164.

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Nagahara, Noriyuki, Masatoshi Nagano, Takaaki Ito, and Hidenori Suzuki. "Redox Regulation of Mammalian 3-Mercaptopyruvate Sulfurtransferase." In Methods in Enzymology, 229–54. Elsevier, 2015. http://dx.doi.org/10.1016/bs.mie.2014.11.017.

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Suwanai, Yusuke, and Noriyuki Nagahara. "Pharmacological usage of a selective inhibitor of 3-mercaptopyruvate sulfurtransferase to control H 2 S and polysulfide generation." In Nanoscale Fabrication, Optimization, Scale-Up and Biological Aspects of Pharmaceutical Nanotechnology, 579–617. Elsevier, 2018. http://dx.doi.org/10.1016/b978-0-12-813629-4.00015-2.

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"Updated Report on a Novel Mercaptopyruvate Sulfurtransferase Thioredoxin-Dependent Redox-Sensing Molecular Switch: A Mechanism for the Maintenance of Cellular Redox Equilibrium." In Recent Advances in Medicinal Chemistry, edited by Noriyuki Nagahara, 56–72. BENTHAM SCIENCE PUBLISHERS, 2014. http://dx.doi.org/10.2174/9781608057962114010005.

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Nagahara, Noriyuki. "Updated Report on a Novel Mercaptopyruvate Sulfurtransferase Thioredoxin-Dependent Redox-Sensing Molecular Switch: A Mechanism for the Maintenance of Cellular Redox Equilibrium." In Recent Advances in Medicinal Chemistry, 56–72. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-803961-8.50002-6.

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