Mildly Oxidized Glyceraldehyde‐3‐Phosphate Dehydrogenase as a Possible Regulator of Glycolysis | Zendy

Danshina P. V. | Zendy; Schmalhausen E. V. | Zendy; Avetisyan A. V. | Zendy; Muronetz V. I. | Zendy

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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 , phosphorylation , incubation

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.

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