Literature DB >> 2597131

Kinetic analysis of protein modification reactions at equilibrium.

E T Rakitzis1.   

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].

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Year:  1989        PMID: 2597131      PMCID: PMC1133509          DOI: 10.1042/bj2630855

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  26 in total

1.  THE REACTIVITIES OF THE HISTIDINE RESIDUES AT THE ACTIVE SITE OF RIBONUCLEASE TOWARD HALO ACIDS OF DIFFERENT STRUCTURES.

Authors:  R L HEINRIKSON; W H STEIN; A M CRESTFIELD; S MOORE
Journal:  J Biol Chem       Date:  1965-07       Impact factor: 5.157

2.  Horse liver alcohol dehydrogenase. A study of the essential lysine residue.

Authors:  S S Chen; P C Engel
Journal:  Biochem J       Date:  1975-09       Impact factor: 3.857

3.  The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.

Authors:  S S Chen; P C Engel
Journal:  Biochem J       Date:  1975-05       Impact factor: 3.857

4.  Half-of-the sites reactivity and negative co-operativity: the case of yeast glyceraldehyde 3-phosphate dehydrogenase.

Authors:  W B Stallcup; D E Koshland
Journal:  J Mol Biol       Date:  1973-10-15       Impact factor: 5.469

5.  Half-of-the sites reactivity in the catalytic mechanism of yeast glyceraldehyde 3-phosphate dehydrogenase.

Authors:  W B Stallcup; D E Koshland
Journal:  J Mol Biol       Date:  1973-10-15       Impact factor: 5.469

6.  Bovine liver glutamate dehydrogenase. Equilibria and kinetics of inactivation by pyridoxal.

Authors:  D Piszkiewicz; E L Smith
Journal:  Biochemistry       Date:  1971-11-23       Impact factor: 3.162

7.  Bovine liver glutamate dehydrogenase. Equilibria and kinetics of imine formation by lysine-97 with pyridoxal 5'-phosphate.

Authors:  D Piszkiewicz; E L Smith
Journal:  Biochemistry       Date:  1971-11-23       Impact factor: 3.162

8.  Properties of the highly reactive SH groups of phosphorylase b.

Authors:  T Sanner; L Tron
Journal:  Biochemistry       Date:  1975-01-28       Impact factor: 3.162

9.  Affinity labelling of rat-muscle hexokinase type II by a glucose-derived alkylating agent.

Authors:  B A Connolly; I P Trayer
Journal:  Eur J Biochem       Date:  1979-01-15

10.  On the function of half-site reactivity: intersubunit NAD+-dependent activation of acyl-glyceraldehyde 3-phosphate dehydrogenase reduction by NADH.

Authors:  B Schwendimann; D Ingbar; S A Bernhard
Journal:  J Mol Biol       Date:  1976-11       Impact factor: 5.469

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  2 in total

1.  Kinetic analysis of regeneration by dilution of a covalently modified protein.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1990-06-15       Impact factor: 3.857

2.  Inactivation of penicillin acylase from Kluyvera citrophila by N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline: a case of time-dependent non-covalent enzyme inhibition.

Authors:  J Martín; J M Mancheño; R Arche
Journal:  Biochem J       Date:  1993-05-01       Impact factor: 3.857

  2 in total

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