ExplorEnz: EC 2.8.1.2

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2.8.1.2

Accepted name:

3-mercaptopyruvate sulfurtransferase

Reaction:

2-oxo-3-sulfanylpropanoate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin (overall reaction)
(1a) 2-oxo-3-sulfanylpropanoate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine = pyruvate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
(1b) [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin = hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin

Glossary:

2-oxo-3-sulfanylpropanoate = 3-mercaptopyruvate (deprecated)

Other name(s):

β-mercaptopyruvate sulfurtransferase; TUM1 (gene name); MPST (gene name); 3-mercaptopyruvate:cyanide sulfurtransferase

Systematic name:

2-oxo-3-sulfanylpropanoate:sulfide sulfurtransferase

Comments:

The enzyme catalyses a transsulfuration reaction from 2-oxo-3-sulfanylpropanoate to an internal cysteine residue. In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-05-5

References:

1.	Fiedler, H. and Wood, J.L. Specificity studies on the β-mercaptopyruvate-cyanide transsulfuration system. J. Biol. Chem. 222 (1956) 387–397. [PMID: 13367011]
2.	Sörbo, B.H. Enzymic transfer of sulfur from mercaptopyruvate to sulfite or sulfinates. Biochem. Biophys. Acta 24 (1957) 324–329. [PMID: 13436433]
3.	Hylin, J.W. and Wood, J.L. Enzymatic formation of polysulfides from mercaptopyruvate. J. Biol. Chem. 234 (1959) 2141–2144. [PMID: 13673028]
4.	van den Hamer, C.J.A., Morell, A.G. and Scheinberg, H.I. A study of the copper content of β-mercaptopyruvate trans-sulfurase. J. Biol. Chem. 242 (1967) 2514–2516. [PMID: 6026243]
5.	Vachek, H. and Wood, J.L. Purification and properties of mercaptopyruvate sulfur transferase of Escherichia coli. Biochim. Biophys. Acta 258 (1972) 133–146. [DOI] [PMID: 4550801]
6.	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 (2005) 34569–34576. [DOI] [PMID: 16107337]
7.	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 (2009) 703–714. [DOI] [PMID: 18855522]
8.	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 (2011) 479–485. [DOI] [PMID: 21732914]

[EC 2.8.1.2 created 1961, modified 2018]