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Subsequently, MPST transfers the persulfide\u2019s 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.<\/jats:p>","DOI":"10.1515\/hsz-2020-0249","type":"journal-article","created":{"date-parts":[[2020,10,20]],"date-time":"2020-10-20T15:46:32Z","timestamp":1603208792000},"page":"223-237","source":"Crossref","is-referenced-by-count":100,"title":["3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking"],"prefix":"10.1515","volume":"402","author":[{"given":"Brand\u00e1n","family":"Pedre","sequence":"first","affiliation":[{"name":"Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ) , Im Neuenheimer Feld 280 , D-69120 Heidelberg , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1367-973X","authenticated-orcid":false,"given":"Tobias P.","family":"Dick","sequence":"additional","affiliation":[{"name":"Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ) , Im Neuenheimer Feld 280 , D-69120 Heidelberg , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2020,10,21]]},"reference":[{"key":"2023040406553385094_j_hsz-2020-0249_ref_001_w2aab3b7b6b1b6b1ab2b2b1Aa","doi-asserted-by":"crossref","unstructured":"Abdollahi Govar, A., T\u00f6r\u0151, G., Szaniszlo, P., Pavlidou, A., Bibli, S.-I., Thanki, K., Resto, V.A., Chao, C., Hellmich, M.R., Szabo, C., et al. (2020). 3-Mercaptopyruvate sulfurtransferase supports endothelial cell angiogenesis and bioenergetics. Br. J.\u00a0Pharmacol. 177: 866\u2013883, https:\/\/doi.org\/10.1111\/bph.14574.","DOI":"10.1111\/bph.14574"},{"key":"2023040406553385094_j_hsz-2020-0249_ref_002_w2aab3b7b6b1b6b1ab2b2b2Aa","unstructured":"Akagi, R. (1982). Purification and characterization of cysteine aminotransferase from rat liver cytosol. Acta Med. Okayama 36: 187\u2013197, https:\/\/doi.org\/10.18926\/AMO\/30697."},{"key":"2023040406553385094_j_hsz-2020-0249_ref_003_w2aab3b7b6b1b6b1ab2b2b3Aa","doi-asserted-by":"crossref","unstructured":"Akahoshi, N., Minakawa, T., Miyashita, M., Sugiyama, U., Saito, C., Takemoto, R., Honda, A., Kamichatani, W., Kamata, S., Anan, Y., et al. (2020). Increased urinary 3-mercaptolactate excretion and enhanced passive systemic anaphylaxis in mice lacking mercaptopyruvate sulfurtransferase, a model of mercaptolactate-cysteine disulfiduria. Int. J.\u00a0Mol. 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