The activation of glycolysis performed by the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system

被引：19

作者：

Arutyunov, DY ^{[1
]}

Muronetz, VI ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, AN Belozersky Inst Phys Chem Biol, Moscow 119992, Russia

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 300卷 / 01期

关键词：

non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; phosphorylating D-glyceraldehyde-3-phosphate; dehydrogenase; regulation of glycolysis; uncoupling of oxidation and phosphorylation; futile cycle; hydrogen peroxide;

D O I：

10.1016/S0006-291X(02)02802-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Influence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) on glycolysis was investigated. The addition of GAPN-which oxidizes glyceraldehyde-3-phosphate directly to the 3-phosphoglyceric acid-led to the strong increase in the rate of lactate accumulation in the rat muscle extract with low ADP content. The lactate accumulation was also observed in the presence of GAPN in rat muscle extract, which contained only ATP and no ADP. This can be the evidence of the "futile cycle" stimulated by GAPN. Here ADP can be regenerated from ATP by the phosphoglycerate kinase reaction. The high resistance of GAPN from Streptococcus mutans towards inactivation by natural oxidant H2O2, was showed. This feature distinguishes GAPN from phosphorylating glyceraldehyde-3-phosphate dehdrogenase, which is very sensitive to modification by hydrogen peroxide. A possible role of the oxidants and non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the regulation of glycolysis is discussed. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：149 / 154

页数：6

共 24 条

[1] Acyl phosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH): a potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells [J].

Albina, JE ;

Mastrofrancesco, B ;

Reichner, JS .

BIOCHEMICAL JOURNAL, 1999, 341 :5-9

[2] SEQUENCE, EXPRESSION, AND FUNCTION OF THE GENE FOR THE NONPHOSPHORYLATING, NADP-DEPENDENT GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE OF STREPTOCOCCUS-MUTANS [J].

BOYD, DA ;

CVITKOVITCH, DG ;

HAMILTON, IR .

JOURNAL OF BACTERIOLOGY, 1995, 177 (10) :2622-2627

[3] OCCURRENCE OF MULTIPLE GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES IN CARIOGENIC STREPTOCOCCI [J].

BROWN, AT ;

WITTENBERGER, CL .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1971, 43 (01) :217-+

[4] NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax -: The first identified archaeal, member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties [J].

Brunner, NA ;

Brinkmann, H ;

Siebers, B ;

Hensel, R .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (11) :6149-6156

[5] Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax:: regulation on protein and transcript level [J].

Brunner, NA ;

Siebers, B ;

Hensel, R .

EXTREMOPHILES, 2001, 5 (02) :101-109

[6]

CROW VL, 1979, J BIOL CHEM, V254, P1134

[7]

Danshina PV, 2001, IUBMB LIFE, V51, P309

[8]

Habenicht A, 1997, BIOL CHEM, V378, P1413

[9] Hydrogen peroxide in the human body [J].

Halliwell, B ;

Clement, MV ;

Long, LH .

FEBS LETTERS, 2000, 486 (01) :10-13

[10] THE HYDROLYSIS OF 1,3-DIPHOSPHOGLYCERIC ACID BY ACYL PHOSPHATASE [J].

HARARY, I .

BIOCHIMICA ET BIOPHYSICA ACTA, 1957, 26 (02) :434-436

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