Acceleration of Glycolysis in the Presence of the Non-phosphorylating and the Oxidized Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenases

P. V. Dan'shina, E. V. Schmalhausen, D. Yu. Arutiunov, A. P. Pleten', and V. I. Muronetz^*

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia; fax: (095) 939-3181; E-mail: vimuronets@belozersky.msu.ru

^* To whom correspondence should be addressed.

Received May 22, 2002

---

Mild oxidation of glyceraldehyde-3-phosphate dehydrogenase in the presence of hydrogen peroxide leads to oxidation of some of the active site cysteine residues to sulfenic acid derivatives, resulting in the induction of acylphosphatase activity. The reduced active sites of the enzyme retain the ability to oxidize glyceraldehyde-3-phosphate yielding 1,3-diphosphoglycerate, while the oxidized active sites catalyze irreversible cleavage of 1,3-diphosphoglycerate. It was assumed that the oxidation of glyceraldehyde-3-phosphate dehydrogenase by different physiological oxidants must accelerate glycolysis due to uncoupling of the reactions of oxidation and phosphorylation. It was shown that the addition of hydrogen peroxide to the mixture of glycolytic enzymes or to the muscle extract increased production of lactate, decreasing the yield of ATP. A similar effect was observed in the presence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase catalyzing irreversible oxidation of glyceraldehyde-3-phosphate into 3-phosphoglycerate. A role of glyceraldehyde-3-phosphate dehydrogenase in regulation of glycolysis is discussed.

---

KEY WORDS:glycolysis, glyceraldehyde-3-phosphate dehydrogenase, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, acylphosphatase activity, hydrogen peroxide, sulfenic acid

---