Influence of Oxidative Stress on Catalytic and Non-glycolytic Functions of Glyceraldehyde-3-phosphate Dehydrogenase

Current Medicinal Chemistry
V I MuronetzE V Schmalhausen

Abstract

Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) is a unique enzyme that, besides its main function in glycolysis (catalysis of glyceraldehyde-3-phosphate oxidation), possesses a number of non-glycolytic activities. The present review summarizes information on the role of oxidative stress in the regulation of the enzymatic activity as well as non-glycolytic functions of GAPDH. Based on the analysis of literature data and the results obtained in our research group, mechanisms of the regulation of GAPDH functions through the oxidation of the sulfhydryl groups in the active site of the enzyme have been suggested. Mechanism of GAPDH oxidation includes consecutive oxidation of the catalytic Cysteine (Cys150) into sulfenic, sulfinic, and sulfonic acid derivatives, resulting in the complete inactivation of the enzyme. The cysteine sulfenic acid reacts with reduced glutathione (GSH) to form a mixed disulfide (S-glutathionylated GAPDH) that further reacts with Cys154 yielding the disulfide bond in the active site of the enzyme. In contrast to the sulfinic and sulfonic acids, the mixed disulfide and the intramolecular disulfide bond are reversible oxidation products that can be reduced in the presence of GSH or thioredoxin. Oxidation of ...Continue Reading

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Citations

May 7, 2020·Pharmaceutics·Vladimir F LazarevBoris A Margulis
May 6, 2020·Current Medicinal Chemistry·Luciano SasoTamas Csont
Nov 26, 2019·Biochemistry. Biokhimii︠a︡·V I MuronetzE V Schmalhausen
Jun 26, 2020·Frontiers in Cell and Developmental Biology·Simona ReinaRosaria Saletti
Jan 21, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Elena Kalinina, Maria Novichkova

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