Literature DB >> 33055309

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

Brandán Pedre1, Tobias P Dick1.   

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.
© 2020 Brandán Pedre and Tobias P. Dick, published by De Gruyter, Berlin/Boston.

Entities:  

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

Year:  2020        PMID: 33055309     DOI: 10.1515/hsz-2020-0249

Source DB:  PubMed          Journal:  Biol Chem        ISSN: 1431-6730            Impact factor:   3.915


  13 in total

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Authors:  Danny Schilling; Uladzimir Barayeu; Raphael R Steimbach; Deepti Talwar; Aubry K Miller; Tobias P Dick
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Review 10.  Antibiotic resistance: The challenges and some emerging strategies for tackling a global menace.

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