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Rabbit muscle GAPDH: non‐phosphorylating dehydrogenase activity induced by hydrogen peroxide
Author(s) -
Elena V. Schmalhausen,
Vladimir I. Muronetz,
N.K. Nagradova
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01044-2
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , sulfenic acid , chemistry , hydrogen peroxide , dehydrogenase , glyceraldehyde , biochemistry , oxidative phosphorylation , enzyme , phosphorylation , phosphate , cysteine
Incubation of glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) with micromolar hydrogen peroxide concentrations does not alter the catalytic properties of GAPDH in the reaction of oxidative phosphorylation of glyceraldehyde‐3‐phosphate, but endows the enzyme with the ability to catalyze the reaction in the absence of inorganic phosphate, producing NADH and 3‐phosphoglycerate. The reaction is supposed to occur as a result of intramolecular acyl transfer from Cys‐149 to a sulfenic acid form of Cys‐153, followed by hydrolysis of the intermediate. The ‘mildly oxidized’ form of the enzyme can be easily converted back to the form unable to catalyze glyceraldehyde‐3‐phosphate oxidation in the absence of phosphate, by the addition of thiols.