Catalytic site cysteines of thiol enzyme: sulfurtransferases.

Journal of Amino Acids
N Nagahara

Abstract

Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active. Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a thiol or a thiolate. The redox changes of these enzymes are involved in their catalytic processes. On the other hand, transferases, and also some phosphatases and hydrolases, have a single-catalytic site cysteine residue. The cysteines are redox active, but their sulfenyl forms, which are inactive, are not well explained biologically. In particular, oxidized forms of sulfurtransferases, such as mercaptopyruvate sulfurtransferase and thiosulfate sulfurtransferase, are not reduced by reduced glutathione but by reduced thioredoxin. This paper focuses on why the catalytic site cysteine of sulfurtransferase is redox active.

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Citations

Jan 23, 2014·Chemical Reviews·Miriam Góngora-BenítezFernando Albericio
Jun 26, 2014·Journal of Analytical Methods in Chemistry·Víctor Pérez Medina MartínezEmilio Medina-Rivero
Apr 7, 2015·Free Radical Biology & Medicine·Young-Mi GoDean P Jones
May 25, 2011·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Piotr SuraMaria Wróbel
Oct 29, 2013·Chemico-biological Interactions·Ling-Ling ChiangUNKNOWN Taiwan CardioPulmonary Research (T-CPR) Group
May 8, 2014·Antioxidants & Redox Signaling·Kenneth R Olson
Oct 23, 2016·Free Radical Biology & Medicine·Ming-Fo HsuTzu-Ching Meng
Jan 4, 2019·American Journal of Physiology. Lung Cellular and Molecular Physiology·Phillip W ClappIlona Jaspers
Nov 18, 2020·Organic & Biomolecular Chemistry·Alane P A Dos SantosFabrício G Menezes

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Methods Mentioned

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