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

Biochemical and Biophysical Research Communications

Volumn 300, Issue 1, 2003, Pages 149-154

  Arutyunov, D Y ^a   Muronetz, V I ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Futile cycle; Hydrogen peroxide; Non phosphorylating glyceraldehyde 3 phosphate dehydrogenase; Phosphorylating D glyceraldehyde 3 phosphate dehydrogenase; Regulation of glycolysis; Uncoupling of oxidation and phosphorylation

Indexed keywords

3 PHOSPHOGLYCERIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCERIC ACID; HYDROGEN PEROXIDE; LACTIC ACID; OXIDIZING AGENT; PHOSPHOGLYCERATE KINASE; UNCLASSIFIED DRUG; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE (NADP);

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; GLYCOLYSIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; RAT; STREPTOCOCCUS MUTANS; ANIMAL; BIOLOGICAL MODEL; COMPARATIVE STUDY; ENZYMOLOGY; IN VITRO STUDY; KINETICS; METABOLISM; MUSCLE; OXIDATION REDUCTION REACTION; PHOSPHORYLATION; RABBIT;

STREPTOCOCCUS; STREPTOCOCCUS MUTANS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE (NADP+); GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; GLYCOLYSIS; KINETICS; LACTIC ACID; MODELS, BIOLOGICAL; MUSCLES; OXIDATION-REDUCTION; PHOSPHORYLATION; RABBITS; RATS; STREPTOCOCCUS MUTANS;

EID: 0037207514     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02802-4     Document Type: Article

References (24)

1. O. Meyerhof, New investigations on enzymatic glycolysis and phosphorylation, Experientia 50 (1994 [1948]) 382-389.
2. I. Harary, The hydrolysis of 1,3-diphosphoglyceric acid by acylphosphatase, Biochim. Biophys. Acta 26 (1957) 434-436.
3. G. Raugei, A. Modesti, F. Magherini, R. Marzocchini, M. Vecchi, G. Ramponi, Expression of acylphosphatase in Saccharomyces cerevisiae enhances ethanol fermentation rate, Biotechnol. Appl. Biochem. 23 (1996) 273-278.
4. E.V. Schmalhausen, V.I. Muronetz, N.K. Nagradova, Rabbit muscle GAPDH: Non-phosphorylating dehydrogenase activity induced by hydrogen peroxide, FEBS Lett. 414 (2) (1997) 247-252.
5. E.V. Schmalhausen, N.K. Nagradova, S. Boschi-Muller, G. Branlant, V.I. Muronetz, Mildly oxidized GAPDH: The coupling of the dehydrogenase and acylphosphatase activities, FEBS Lett. 452 (1999) 219-222.
6. P.V. Danshina, E.V. Schmalhausen, A.V. Avetisyan, V.I. Muronetz, Mildly oxidized glyceraldehyde-3-phosphate dehydrogenase as a possible regulator of glycolysis, IUBMB Life 51 (2001) 309-314.
7. A. Habenicht, The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase: Biochemistry, structure, occurrence and evolution, Biol. Chem. 378 (1997) 1413-1419.
8. F. Valverde, M. Losada, A. Serrano, Engineering a central methabolic pathway: Glycolysis with no net phosphorylation in an Escherichia coli gap mutant complemented with a plant GapN gene, FEBS Lett. 449 (1999) 153-158.
9. R.K. Scopes, A. Stoter, Purification of all glycolytic enzymes from one muscle extract, in: Methods in Enzymology, vol. 90, Academic press, New York, 1982, pp. 479-491.
10. V.L. Crow, C.L. Wittenberger, Separation and properties of NAD- and NADP-dependent glyceraldehydes-3-phosphate dehydrogenases from Streptococcus mutans, J. Biol. Chem. 254 (1979) 1134-1142.
11. S. Marchal, G. Branlant, Evidence for the chemical activation of essential Cys-302 upon cofactor binding to non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans, Biochemistry 38 (1999) 12950-12958.
12. A. Serrano, M.I. Mateos, M. Losada, ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenases (phosphorylating and non-phosphorylating) model system, Biochem. Biophys. Res. Commun. 197 (3) (1993) 1348-1356.
13. P.A. Hyslop, D.B. Hinshaw, W.A. Halsey Jr., I.U. Schraufstatter, R.D. Sauerheber, R.G. Spragg, J.H. Jackson, C.G. Cochrane, Mechanisms of oxidant-mediated cell injury, J. Biol. Chem. 263 (1988) 1665-1675.
14. E.V. Schmalhausen, V.I. Muronetz, An uncoupling of the processes of oxidation and phosphorylation in glycolysis, Biosci. Rep. 17 (1997) 521-527.
15. B. Halliwell, M.V. Clement, L.H. Long, Hydrogen peroxide in the human body, FEBS Lett. 486 (2000) 10-13.
16. A.T. Brown, C.L. Wittenberger, The occurrence of multiple glyceraldehydes-3-phosphate dehydrogenases in cariogenic streptococci, Biochem. Biophys. Res. Commun. 43 (1) (1971) 217-224.
17. E.V. Kuzminskaya, R.A. Asryants, N.K. Nagradova, Rabbit muscle tetrameric D-glyceraldehyde-3-phosphate dehydrogenase is locked in the asymmetric state by chemical modification of a single arginine per subunit, Biochim. Biophys. Acta 1075 (1991) 123-130.
18. G.E. Albina, B. Mastrofrancesco, J.S. Reichner, Acylphosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH): A potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells, Biochem. J. 341 (1999) 5-9.
19. N.A. Brunner, H. Brinkmann, B. Siebers, R. Hensel, 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. Biol. Chem. 273 (11) (1998) 6149-6156.
20. N.A. Brunner, B. Siebers, R. Hensel, 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, Extremophiles 5 (2001) 101-109.
21. J. van der Oost, G. Schut, S.W.M. Kengen, W.R. Hageni, M. Thomm, W.M. de Vos, The ferredoxin-dependent conversion of glyceraldehyde-3 phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation, J. Biol. Chem. 273 (43) (1998) 28149-28154.
22. S.W.M. Kengen, W.M. de Vos, A.J.M. Stams, Sugar metabolism of hyperthermophiles, FEMS Microbiol. Rev. 18 (1996) 119-137.
23. D.A. Boyd, D.G. Cvitkovitch, I.R. Hamilton, Sequence, expression and function of the gene for the non-phosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans, J. Bacteriol. 177 (10) (1995) 2622-2627.
24. M. Solti, P. Friedrich, The "enzyme-probe" method for characterizating metabolite pools. The use of NAD-glycohydrolase in human erythrocyte sonicate as a model system, Eur. J. Biochem. 95 (1979) 551-559.