Regulation of mercaptopyruvate sulfurtransferase activity via intrasubunit and intersubunit redox-sensing switches

Antioxidants and Redox Signaling

Volumn 19, Issue 15, 2013, Pages 1792-1802

  Nagahara, Noriyuki ^a  

^a NIPPON MEDICAL SCHOOL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 MERCAPTOPYRUVATE SULFURTRANSFERASE; 3 MERCAPTOPYRUVIC ACID; CYSTEINE; HYDROGEN SULFIDE; SULFUR OXIDE; SULFURTRANSFERASE; THIOREDOXIN PEROXIDASE; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

BEHAVIOR CHANGE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME REGULATION; INBORN ERROR OF METABOLISM; INTERSUBUNIT REDOX SENSING SWITCH; INTRASUBUNIT REDOX SENSING SWITCH; MERCAPTOLACTATE CYSTEINE DISULFIDURIA; MOLECULAR EVOLUTION; MOUSE; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PATHOGENESIS; PRIORITY JOURNAL; REGULATORY MECHANISM; REVIEW; SEQUENCE HOMOLOGY;

ANIMALS; BIOSENSING TECHNIQUES; CATALYSIS; CYSTEINE; ENZYME ACTIVATION; EVOLUTION, MOLECULAR; HUMANS; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; SULFURTRANSFERASES;

EID: 84879682497     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.5031     Document Type: Review

References (25)

1. Ampola MG, Efron ML, Bixby E.M., and Meshorer E. Mental deficiency and a new aminoaciduria. Am J Dis Child 117: 66-70, 1969.
2. Aslund F, Berndt KD, and Holmgren A. Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. J Biol Chem 272: 30780-30786, 1997.
3. Brenner S, Elgar G, Sandford R., Macrae A, Venkatesh B, and Aparicio S. Characterization of the pufferfish (Fugu) genome as a compact model vertebrate genome. Nature 366: 265-268, 1993. (Pubitemid 23359708)
4. Canfield DE. The early history of atmospheric oxygen. Annu Rev Earth Planet Sci 33: 1-3, 2005.
5. Crawhall JC, Parker R. Young EP, Ampola MG, Efron ML, and Bixby EM. Beta mercaptolactate-cysteine disulfide: analog of cystine in the urine of a mentally retarded patient. Science 160: 419-420, 1968.
6. 3- radicals in aqueous solution. J Phys Chem A 103: 3581-3588, 1999.
7. Horowitz PM and Criscimagna NL. Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese. J Biol Chem 263: 10278-10283, 1988.
8. Kasting JF and Siefert JL. Life and the evolution of Earth's atmosphere. Science 296: 1066-1068, 2002. (Pubitemid 34517114)
9. Linke K and Jakob U. Not every disulfide lasts forever: disulfide bond formation as a redox switch. Antioxid Redox Signal 5: 425-434, 2003. (Pubitemid 37087402)
10. Meister A. Conversion of the α-keto analog of cysteine to pyruvate and sulfur. Fed Proc 12: 245, 1953.
11. Mikami Y, Shibuya N, Kimura Y., Nagahara N, Ogasawara Y, and Kimura H. Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochem J 439: 479-486, 2011.
12. Nagahara N and Katayama A. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis. J Biol Chem 280: 34569-23576, 2005.
13. Nagahara N and Nishino T. Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. cDNA cloning, overexpression, and site-directed mutagenesis. J Biol Chem 271: 27395-427401, 1996.
14. Nagahara N and Sawada N. The mercaptopyruvate pathway in cysteine catabolism: a physiologic role and related disease of the multifunctional 3-mercaptopyruvate sulfurtransferase. Curr Med Chem 13: 1219-1930, 2006.
15. Nagahara N, Ito T, and Minami M. Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: Molecular properties and mode of detoxification. Histol Histopathol 14: 1277-1286, 1999. (Pubitemid 29447468)
16. Nagahara N, Ito T, Kitamura H., and Nishino T. Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis. Histochem Cell Biol 110: 243-250, 1998. (Pubitemid 28401732)
17. Nagahara N, Nirasawa T, Yoshii T., and Niimura Y. Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase? Antioxid Redox Signal 16: 747-753, 2012.
18. Nagahara N, Okazaki T, and Nishino T. Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis. J Biol Chem 270: 16230-16235, 1995.
19. Nagahara N, Sreeja VG, Li Q, Shimizu T., Tsuchiya T, and Fujii-Kuriyama Y. A point mutation in a silencer module reduces the promoter activity for the human mercaptopyruvate sulfurtransferase. Biochim Biophys Acta 1680: 176-184, 2004. (Pubitemid 39422713)
20. Nagahara N, Yoshii T, Abe Y., and Matsumura T. Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. J Biol Chem 282: 1561-1569, 2007. (Pubitemid 47076697)
21. Nakamura T, Yamaguchi Y, and Sano H. Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities. Eur J Biochem 267: 5621-5630, 2000.
22. Sawada N, Nagahara N, Sakai T., Nakajima Y, Minami M, and Kawada T. The activationmechanism of human porphobilinogen synthase by 2-mercaptoethanol: intrasubunit transfer of a reserve zinc ion and coordination. J Biol Inorg Chem 10: 199-207, 2005. (Pubitemid 40569014)
23. Shibuya N, Tanaka M, Yoshida M., Ogasawara Y, Togawa T, Ishii K., and Kimura H. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal 11: 703-714, 2009.
24. Spallarossa A, Forlani F, Carpen A., Armirotti A, Pagani S, Bolognesi M., and Bordo D. The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli. J Mol Biol 335: 583-593, 2004. (Pubitemid 37532658)
25. Wood JL and Fiedler H. Beta-Mercapto-pyruvate, a substrate for rhodanese. J Biol Chem 205: 231-234, 1953.