3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking
Author:
Pedre Brandán1, Dick Tobias P.1ORCID
Affiliation:
1. Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ) , Im Neuenheimer Feld 280 , D-69120 Heidelberg , Germany
Abstract
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.
Funder
Deutsche Forschungsgemeinschaft
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Reference99 articles.
1. Abdollahi Govar, A., Törő, 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. Pharmacol. 177: 866–883, https://doi.org/10.1111/bph.14574. 2. Akagi, R. (1982). Purification and characterization of cysteine aminotransferase from rat liver cytosol. Acta Med. Okayama 36: 187–197, https://doi.org/10.18926/AMO/30697. 3. 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. Mol. Sci. 21, https://doi.org/10.3390/ijms21030818. 4. Augsburger, F., Randi, E.B., Jendly, M., Ascencao, K., Dilek, N., and Szabo, C. (2020). Role of 3-mercaptopyruvate sulfurtransferase in the regulation of proliferation, migration, and bioenergetics in murine colon cancer cells. Biomolecules 10: 447, https://doi.org/10.3390/biom10030447. 5. Bian, Y., Song, C., Cheng, K., Dong, M., Wang, F., Huang, J., Sun, D., Wang, L., Ye, M., and Zou, H. (2014). An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics 96: 253–262, https://doi.org/10.1016/j.jprot.2013.11.014.
Cited by
57 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
|
|