Kinetic analysis of protein modification reactions at equilibrium
- PMID: 2597131
- PMCID: PMC1133509
- DOI: 10.1042/bj2630855
Kinetic analysis of protein modification reactions at equilibrium
Abstract
A kinetic analysis is presented of reactions of protein modification, and/or of modification-induced enzyme inactivation, which can formally be described by a single exponential function, or by a summation of two exponential functions, of reaction time plus a constant term. The reaction schemes compatible with the kinetic formalism of these cases are given, and a simple kinetic criterion is described whereby the identification of one of these cases, strong negative protein modification co-operativity, may be carried out. The treatment outlined in this paper is applied to a case from the literature, the inactivation of glyceraldehyde-3-phosphate dehydrogenase by butane-2,3-dione [Asriyants, Benkevich & Nagradova (1983) Biokhimiya (Engl. Transl.) 48, 164-171].
Similar articles
-
Kinetic analysis of biphasic protein modification reactions. Cooperative effects.Biophys Chem. 1983 Sep;18(2):133-7. doi: 10.1016/0301-4622(83)85007-8. Biophys Chem. 1983. PMID: 6626686
-
E. coli D-glyceraldehyde-3-phosphate dehydrogenase modified by 2,3-butanedione: manifestation of a pairwise of non-equivalence of active centers.Biochem Mol Biol Int. 1995 Nov;37(5):991-1000. Biochem Mol Biol Int. 1995. PMID: 8624507
-
Effect of coenzymes on the quaternary structure conformation of glyceraldehyde-3-phosphate dehydrogenases of mung beans and rabbit muscle.Indian J Biochem Biophys. 1992 Dec;29(6):469-76. Indian J Biochem Biophys. 1992. PMID: 1294463
-
The hybridization of glyceraldehyde 3-phosphate dehydrogenases from rabbit muscle and yeast. Kinetics and thermodynamics of the reaction and isolation of the hybrid.Biochem J. 1974 Dec;143(3):651-62. doi: 10.1042/bj1430651. Biochem J. 1974. PMID: 4618477 Free PMC article.
-
The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase: biochemistry, structure, occurrence and evolution.Biol Chem. 1997 Dec;378(12):1413-9. Biol Chem. 1997. PMID: 9461340 Review.
Cited by
-
Inactivation of penicillin acylase from Kluyvera citrophila by N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline: a case of time-dependent non-covalent enzyme inhibition.Biochem J. 1993 May 1;291 ( Pt 3)(Pt 3):907-14. doi: 10.1042/bj2910907. Biochem J. 1993. PMID: 8489517 Free PMC article.
-
Kinetic analysis of regeneration by dilution of a covalently modified protein.Biochem J. 1990 Jun 15;268(3):669-70. doi: 10.1042/bj2680669. Biochem J. 1990. PMID: 2363704 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials