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Review
. 2020 Oct 21;402(3):223-237.
doi: 10.1515/hsz-2020-0249. Print 2021 Feb 23.

3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking

Brandán Pedre  1 , Tobias P Dick  1
Affiliations
Free article
Review

3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking

Brandán Pedre et al. Biol Chem. .
Free article

Abstract

3-Mercaptopyruvate sulfurtransferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate to generate an enzyme-bound hydropersulfide. Subsequently, MPST transfers the persulfide's outer sulfur atom to proteins or small molecule acceptors. MPST activity is known to be involved in hydrogen sulfide generation, tRNA thiolation, protein urmylation and cyanide detoxification. Tissue-specific changes in MPST expression correlate with ageing and the development of metabolic disease. Deletion and overexpression experiments suggest that MPST contributes to oxidative stress resistance, mitochondrial respiratory function and the regulation of fatty acid metabolism. However, the role and regulation of MPST in the larger physiological context remain to be understood.

Keywords: 3-mercaptopyruvate; 3-mercaptopyruvate sulfur transferase; hydrogen sulfide; persulfides; rhodanese superfamily; sulfane sulfur.

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