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Mini-Reviews in Medicinal Chemistry


ISSN (Print): 1389-5575
ISSN (Online): 1875-5607

A Novel Mercaptopyruvate Sulfurtransferase Thioredoxin-Dependent Redox-Sensing Molecular Switch: A Mechanism for the Maintenance of Cellular Redox Equilibrium

Author(s): Noriyuki Nagahara

Volume 8, Issue 6, 2008

Page: [585 - 589] Pages: 5

DOI: 10.2174/138955708784534409

Price: $65


An intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase (MST, EC. A cysteine residue on the surface of each subunit was oxidized to form an intersubunit disulfide bond so as to decrease MST activity, and thioredoxin-specific conversion of a dimer to a monomer increased MST activity. Further, a low redox potential sulfenate was reversibly formed at a catalytic site cysteine so as to inhibit MST, and thioredoxin-dependent reduction of the sulfenate restored the MST activity. Concludingly, MST partly contributes to the maintenance of cellular redox homeostasis via exerting control over cysteine catabolism.

Keywords: Atmospheric oxygen, antioxidative stress, intermolecular disulfide bond, mercaptolactate-cysteine disulfiduria, mercaptopyruvate sulfurtransferase, molecular evolution, redox-sensing switch, thioredoxin

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