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Mildly Oxidized Glyceraldehyde‐3‐Phosphate Dehydrogenase as a Possible Regulator of Glycolysis
Author(s) -
Danshina P. V.,
Schmalhausen E. V.,
Avetisyan A. V.,
Muronetz V. I.
Publication year - 2001
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/152165401317190824
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , glycolysis , dehydrogenase , biochemistry , anaerobic glycolysis , glyceraldehyde , oxidative phosphorylation , enzyme , chemistry , lactate dehydrogenase , incubation , phosphorylation , citric acid cycle
Abstract Influence of H 2 O 2 on glycolysis was investigated. A hypothesis previously formulated was tested according to which a mild oxidation of glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) results in uncoupling of oxidation and phosphorylation at this step of glycolysis due to acylphosphatase activity of the oxidized enzyme. Incubation of a mixture of purified glycolytic enzymes, as well as a muscle extract, in the presence of 10‐100 μMH 2 O 2 was shown to result in an increase in the rate of glycolysis. The level of lactate accumulation in the oxidized samples increased by 80‐150% compared to the samples containing mercaptoethanol. No ATP was formed by the H 2 O 2 ‐stimulated glycolysis. Thus, H 2 O 2 really caused uncoupling of oxidation and phosphorylation in glycolysis. A role of GAPDH oxidation in regulation of glycolysis is discussed.