The Kinetic Investigation of D-Hydroxyisovalerate Dehydrogenase from Fusarium sambucinum

Journal of Biochemistry and Molecular Biology

Volumn 33, Issue 3, 2000, Pages 228-233

  Lee, Chan ^a   Goerisch, Helmut ^b   Zocher, Rainer ^b  

^a Chung Ang University   (South Korea)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

D Hydroxyisovalerate dehydrogenase; Eniatin; Kinetic mechanism

Indexed keywords

EID: 0034400622     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Akimenko, V. K., Andreeva, N. A., Kulaev, I. S., Lozinov, A. B. and Chermenskii, D. N. (1981) Interrelationship between enniatin synthesis, ATP pool, and cynide-resistant respiration. Mikbrobiologiya 50, 205-210.
2. Audhya, T. K. and Russel, D. W. (1973) Production of enniatin A. Can. J. Microbial. 19, 1051-1054.
3. Bradbury S. L. and Jakoby, W. B. (1971) Ordered binding of substrates to yeast aldehyde dehydrogenase. J. Biol. Chem. 246, 1834-1840.
4. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
5. + oxidoreductase. Eur. J. Biochem. 116, 137-142.
6. Dean. A. M., Lee, M. H. I. and Koshland, Jr. D. E. (1989) Phosphorylation inactivates Escherichla coli isocitrate dehydrogenase by preventing isocitrate binding. J. Biol Chem. 264, 20482-20486.
7. Dugan, E. R. and Porter, J. W. (1971) Mechanism of binding of reduced nicotinamide adennine dinucleotide phosphate to vertebrate fatty acid synthetases. J. Biol. Chem. 246, 637-642.
8. Duggleby, G. G. and Pang S. S. (2000) Acetohydroxyacid synthetase. J. Biochem. Mol. Biol. 33, 1-36.
9. Feldman, R. J. and Weiner, H. (1972) Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity. J. Biol. Chem. 247, 267-272.
10. Hsu, R. Y., Lardy, H. A. and Cleland, W. W. (1967) Pigeon liver malic enzyme. V. Kinetic studies. J. Biol. Chem. 242, 5315-5322.
11. Hwang, S. I. and Lim, J. K. (1999) Purification of bovine pregnancy-associated proteins by two dimensional gel electrophoresis. J. Biochem. Mol. Biol. 32, 445-450.
12. Kim, K. S. and Suk, H. W. (1998) Biochemical properties of NAD(P)H-quinone oxidoreductase from Saccharomyces cerevisiae. J. Biochem. Mol. Biol. 32, 127-132.
13. Lee, C., Goerisch, H., Kleinkauf, H. and Zocher, R. (1992) A highly specific D-hydroxyisovalerate dehydrogenase from the enniatin producer Fusariuin sambucinum. J. Biol. Chem. 267, 11741.
14. Lee, C. and Zocher, R. (1996) The biochemical characterization of D-hydroxyisovalerate dehydrogenase, a key enzyme in the biosynthesis of enniatins. J. Biochem. Mol. Biol. 29, 493-499.
15. Madry, N., Zocher, R. and Kleinkauf, H. (1983) Enniatin puction by Fusariuin oxysporum in chemically defined media. Eur. J. Microbiol. Biotechnol. 17, 75-79.
16. Ordmann, A. B. and Kirkwood, S. (1977) UDP glucose dehydrogenase. Kinetics and their mechanistic implications. Biochim. Biophys. Acta 481, 25-32.
17. Orsi, B. A. and Cleland, W. W. (1972) Inhibition and kinetic mechanism of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 11, 102-109.
18. Peacock, D. and Boulter, D. (1970) Kinetic studies of formate dehydrogenase. Biochem. J. 120, 763-769.
19. Peeters, H., Zocher, R., Madry, N., Oelrichs, P. B., Kleinkauf, H. and Kraepelin, G. (1983) Cell-free synthesis of the depsipeptide beauvericin. J. antibiot. 36, 1762-1766.
20. Ruediger, H. W., Langenbeck, U. and Goedde, H. W. (1972) A simplified method for the preparation of 14 C-labeled branched chain oxoacids. Biochem. J. 126, 445-446.
21. Segel, I. H. (1975a) General rules for defining kinetic constants and deriving velocity equations : Cleland nomenclature, pp 523-533; In Enzyme kinetics, Wiley Interscience Publications, New York.
22. Segel, I. H. (1975b) The King-Altman method of deriving steady-state velocity equations, pp 506-522; In Enzyme kinetics, Wiley Interscience Publications, New York.
23. Segel, I. H. (1975c) Steady-state kinetics of multireactant enzymes, pp 534-657; In Enzyme kinetics, Wiley Interscience Publications, New York.
24. Smith, G. D., Duax, W. L., Langs, D. A., Detitta, G. T., Edmonds, J. W., Rohrer, D. C. and Weeks, C. M. (1975) The crystal and molecular structure of the triclinic and monoclinic forms of valinomycin, C54H90N6O18. J. Am. Chem. Soc. 97, 7242-7247.
25. Zocher, R., Keller, U. and Kleinkauf, H. (1982) Enniatin synthetase, a novel type of multifunctional enzyme catalyzing depsipeptide synthesis in Fusarium oxysporum. Biochemistry 21, 43-48.