Literature DB >> 6497841

Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity.

E T Rakitzis.   

Abstract

The plot of fractional enzyme activity versus extent of protein modification, for cases where all enzyme modifiable groups of a certain kind are essential for activity, is found to be nearly independent of the number, per enzyme active site, of modifiable groups involved. Such plots usually, by a fallacious extension of the initial portion of the plot on the extent-of-modification axis, are interpreted to mean the modification of one single group per enzyme active site (or per enzyme molecule). The possible relevance of these findings to cases in the literature is discussed.

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Year:  1984        PMID: 6497841      PMCID: PMC1144288          DOI: 10.1042/bj2230259

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


  18 in total

1.  The specificity of induced conformational changes. The case of yeast glyceraldehyde-3-phosphate dehydrogenase.

Authors:  L D Byers; D E Koshland
Journal:  Biochemistry       Date:  1975-08-12       Impact factor: 3.162

2.  Functional arginine residues involved in coenzyme binding by glutamate dehydrogenases.

Authors:  K M Blumenthal; E L Smith
Journal:  J Biol Chem       Date:  1975-08-25       Impact factor: 5.157

3.  Studies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli.

Authors:  K Mizuta; M Tokushige
Journal:  Biochim Biophys Acta       Date:  1975-09-22

4.  Kinetics of irreversible enzyme inhibition: co-operative effects.

Authors:  E T Rakitzis
Journal:  J Theor Biol       Date:  1977-07-07       Impact factor: 2.691

5.  An essential residue at the active site of aspartate transcarbamylase.

Authors:  E R Kantrowitz; W N Lipscomb
Journal:  J Biol Chem       Date:  1976-05-10       Impact factor: 5.157

6.  A single functional arginyl residue involved in the catalysis promoted by Lactobacillus casei thymidylate synthetase.

Authors:  M Belfort; G F Maley; F Maley
Journal:  Arch Biochem Biophys       Date:  1980-10-01       Impact factor: 4.013

7.  Reactivity of sulfhydryl groups of the flavoenzyme D-lactate dehydrogenase and effect on catalytic activity.

Authors:  S T Olson; V Massey
Journal:  Biochemistry       Date:  1980-07-08       Impact factor: 3.162

8.  Comparison of experimental binding data and theoretical models in proteins containing subunits.

Authors:  D E Koshland; G Némethy; D Filmer
Journal:  Biochemistry       Date:  1966-01       Impact factor: 3.162

Review 9.  Arginyl residues and anion binding sites in proteins.

Authors:  J F Riordan
Journal:  Mol Cell Biochem       Date:  1979-07-31       Impact factor: 3.396

10.  Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrophosphatase.

Authors:  M W Bond; N Y Chiu; B S Cooperman
Journal:  Biochemistry       Date:  1980-01-08       Impact factor: 3.162

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  4 in total

1.  Kinetics of protein-modification reactions. Determination of the fractional concentration of enzyme protein groups, or group reactivities, essential for catalytic function.

Authors:  E T Rakitzis; T B Malliopoulou
Journal:  Biochem J       Date:  1986-07-15       Impact factor: 3.857

2.  Identification of an essential glutamic acid residue in beta-lactamase II from Bacillus cereus.

Authors:  C Little; E L Emanuel; J Gagnon; S G Waley
Journal:  Biochem J       Date:  1986-01-15       Impact factor: 3.857

3.  Kinetics of protein-modification reactions. Stoichiometry of modification-produced enzyme inactivation: modification of rhodanese by 2,4,6-trinitrobenzenesulphonic acid.

Authors:  E T Rakitzis; T B Malliopoulou
Journal:  Biochem J       Date:  1985-08-15       Impact factor: 3.857

4.  Kinetics of protein modification and enzyme inactivation reactions: interpretation of reaction order.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1985-10-15       Impact factor: 3.857

  4 in total

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