Identification of the kinetic mechanism of succinyl-CoA synthetase

Bioscience Reports

Volumn 33, Issue 1, 2013, Pages 145-163

  Li, Xin ^a   Wu, Fan ^a   Beard, Daniel A ^a  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

Catalytic mechanism; Dead end binding; Enzyme; Succinyl CoA

Indexed keywords

COENZYME A; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PHOSPHATE; PROTON; SUCCINIC ACID; SUCCINYL COENZYME A SYNTHETASE;

ARTICLE; BINDING KINETICS; CHEMICAL INTERACTION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; IONIC STRENGTH; MATHEMATICAL MODEL; NONHUMAN; SENSITIVITY ANALYSIS; SIMULATION; SWINE; THERMODYNAMICS;

ACYL COENZYME A; ANIMALS; COMPUTER SIMULATION; ENZYME STABILITY; KINETICS; MYOCARDIUM; OSMOLAR CONCENTRATION; PHOSPHORYLATION; PROTEIN BINDING; SENSITIVITY AND SPECIFICITY; SUCCINATE-COA LIGASES; SUCCINIC ACID; SWINE; THERMODYNAMICS;

SUS;

EID: 84872705578     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20120069     Document Type: Article

References (32)

1. Bridger, W. A. (1974) Succinyl-CoA synthetase. In The Enzymes (Boyer, P. D., ed.), pp. 581-606, Academic Press, London/New York
2. Joyce, M. A. (2000) Structural and Functional Studies of Succinyl-CoA Synthetase. Ph. D. Thesis University of Alberta, Edmonton, AB, Canada
3. Labbe, R. F., Kurumada, T. and Onisawa, J. (1965) The role of succinyl-CoA synthetase in the control of heme biosynthesis. Biochim. Biophys. Acta 111, 403-415
4. Alarcon, C., Wicksteed, B., Prentki, M., Corkey, B. E. and Rhodes, C. J. (2002) Succinate is a preferential metabolic stimulus-coupling signal for glucose-induced proinsulin biosynthesis translation. Diabetes 51, 2496-2504
5. Fahien, L. A. and MacDonald, M. J. (2002) The succinate mechanism of insulin release. Diabetes 51, 2669-2676
6. Brìere, J. J., Favier, J., Gimenez-Roqueplo, A. P. and Rustin, P. (2006) Tricarboxylic acid cycle dysfunction as a cause of human diseases and tumor formation. Am. J. Physiol. Cell Physiol. 291, C1114-C1120
7. Kaufman, S. (1955) Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme. J. Biol. Chem. 216, 153-164
8. Cha, S. and Parks, Jr, R. E. (1964) Succinic thiokinase. II. Kinetic studies: initial velocity, product inhibition, and effect of arsenate. J. Biol. Chem. 239, 1968-1977
9. Cha, S., Cha, C. J. and Parks, Jr, R. E. (1965) Succinic thiokinase. 3. The occurrence of a nonphosphorylated high energy intermediate of the enzyme. J. Biol. Chem. 240, 3700-3702
10. Moyer, R. W., Ramaley, R. F., Butler, L. G. and Boyer, P. D. (1967) The formation and reactions of a nonphosphorylated high energy form of succinyl coenzyme A synthetase. J. Biol. Chem. 242, 4299-4309
11. Hager, L. P. (1962) Succinyl CoA synthetase. In The Enzymes (Boyer, P. D., Lardy, H. and Myrback, K., eds), pp. 387-394, Academic Press, London/New York
12. Nishimura, J. S. (1986) Succinyl-CoA synthetase structure-function relationships and other considerations. Adv. Enzymol. Relat. Areas Mol. Biol. 58, 141-172
13. Nishimura, J. S., Manning, J. M. and Meister, A. (1962) Studies on the mechanism of activation acid beta-decarboxylase by alpha-keto acids and pyridoxal 5-phosphate. Biochemistry 1, 442-447
14. Kohn, M. C., Achs, M. J. and Garfinkel, D. (1979) Computer simulation of metabolism in pyruvate-perfused rat heart. II. Krebs cycle. Am. J. Physiol. Regul. Integr. Comp. Physiol. 237, R159-R166
15. Moffet, F. J. and Bridger, W. A. (1973) Succinyl coenzyme A synthetase of Escherichia coli: initial rate kinetics of succinyl-CoA cleavage and isotope exchange studies. Can. J. Biochem. 51, 44-55
16. Moffet, R. J. and Bridger, W. A. (1970) The kinetics of succinyl coenzyme A synthetase from Escherichia coli. A reaction with a covalent enzyme-substrate intermediate not exhibiting 'ping-pong' kinetics. J. Biol. Chem. 245, 2758-2762
17. Beard, D. A., Vinnakota, K. C. and Wu, F. (2008) Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. PLoS ONE 3, e1825
18. Mescam, M., Vinnakota, K. C. and Beard, D. A. (2011) Identification of the catalytic mechanism and estimation of kinetic parameters for fumarase. J. Biol. Chem. 286, 21100-21109
19. Li, X., Wu, F., Qi, F. and Beard, D. A. (2011) A database of thermodynamic properties of the reactions of glycolysis, the tricarboxylic acid cycle, and the pentose phosphate pathway. Database (Oxford) 2011, bar005
20. Li, X., Dash, R. K., Pradhan, R. K., Qi, F., Thompson, M., Vinnakota, K. C., Wu, F., Yang, F. and Beard, D. A. (2010) A database of thermodynamic quantities for the reactions of glycolysis and the tricarboxylic acid cycle. J. Phys. Chem. B 114, 16068-16082
21. Beard, D. A. and Qian, H. (2008) Conventions and calculations for biochemical systems. In Chemical Biophysics: Quantitative Analysis of Cellular Systems, pp. 24-40, Cambridge University Press, Cambridge
22. Alberty, R. A. (2003) Thermodynamics of Biochemical Reactions, Wiley-Interscience, Hoboken
23. Johnson, J. D., Mehus, J. G., Tews, K., Milavetz, B. I. and Lambeth, D. O. (1998) Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J. Biol. Chem. 273, 27580-27586
24. Fraser, M. E., James, M. N., Bridger, W. A. and Wolodko, W. T. (2000) Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase. J. Mol. Biol. 299, 1325-1339
25. Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta 67, 104-137
26. Segel, I. H. (1993) Enzyme Kinetics, Wiley Classics Library edition, Wiley Interscience, New York
27. Cha, S. and Parks, Jr, R. E. (1964) Succinic thiokinase. I. Purification of the enzyme from pig heart. J. Biol. Chem. 239, 1961-1967
28. Bergman, R. N., Ider, Y. Z., Bowden, C. R. and Cobelli, C. (1979) Quantitative estimation of insulin sensitivity. Am. J. Physiol. 236, E667-E677
29. Bridger, W. A., Millen, W. A. and Boyer, P. D. (1968) Substrate synergism and phosphoenzyme formation in catalysis by succinyl coenzyme A synthetase. Biochemistry 7, 3608-3616
30. Grinnell, F. and Nishimura, J. S. (1969) Studies on the catalytic mechanism of Escherichia coli succinic thiokinase. Biochemistry 8, 4126-4130
31. Fraser, M. E., James, M. N., Bridger, W. A. and Wolodko, W. T. (1999) A detailed structural description of Escherichia coli succinyl-CoA synthetase. J. Mol. Biol. 285, 1633-1653
32. Phillips, D., Aponte, A. M., French, S. A., Chess, D. J. and Balaban, R. S. (2009) Succinyl-CoA synthetase is a phosphate target for the activation of mitochondrial metabolism. Biochemistry 48, 7140-7149