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Literature DB >> 4206910

Inhibition of enzymes by metal ion-chelating reagents. Theory and new graphical methods of study.

Abstract

1. The mechanism of inhibition of enzymes by metal ion-chelating reagents is discussed and equations derived. 2. Two distinct mechanisms are postulated and graphical methods are given for differentiating between them. 3. Where the metal ion is actually removed from the enzyme to form a co-ordination complex in solution, a procedure is described for obtaining the stability constant for metal-enzyme interaction, the number of metal ions involved and the stoicheiometry of metal ion-ligand interaction.

Entities: Chemical

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Year: 1974 PMID： 4206910 PMCID： PMC1166079 DOI： 10.1042/bj1370055

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

7 in total

1. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection.

Authors: W W CLELAND
Journal: Biochim Biophys Acta Date: 1963-02-12

2. The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule.

Authors: J H KAGI; B L VALLEE
Journal: J Biol Chem Date: 1960-11 Impact factor: 5.157

3. The role of zinc in alcohol dehydrogenases. III. The kinetics of a time-dependent inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.

Authors: R J WILLIAMS; F L HOCH; B L VALLEE
Journal: J Biol Chem Date: 1958-05 Impact factor: 5.157

4. The role of zinc in alcohol dehydrogenases. II. The kinetics of the instantaneous reversible inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.

Authors: F L HOCH; R J WILLIAMS; B L VALLEE
Journal: J Biol Chem Date: 1958-05 Impact factor: 5.157

4. Correlation of the effects of citric acid cycle metabolites on succinate oxidation by rat liver mitochondria and submitochondrial particles.

Authors: M Hillar; V Lott; B Lennox
Journal: J Bioenerg Date: 1975-03

5. The glycoprotein nature of pig kidney diamine oxidase. Role of disulphide groups and arginine residues in the concanavalin A-diamine oxidase interaction.

Authors: M A Shah; R Ali
Journal: Biochem J Date: 1988-07-01 Impact factor: 3.857

6. Inhibition of enzymes by metal ion-chelating reagents. The action of copper-chelating reagents on diamine oxidase.

Authors: W G Bardsley; R E Childs; M J Crabbe
Journal: Biochem J Date: 1974-01 Impact factor: 3.857

7. Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase.

Authors: N J Blackburn; D Collison; J Sutton; F E Mabbs
Journal: Biochem J Date: 1984-06-01 Impact factor: 3.857

7 in total

Inhibition of enzymes by metal ion-chelating reagents. Theory and new graphical methods of study.

1. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection.

2. The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule.

3. The role of zinc in alcohol dehydrogenases. III. The kinetics of a time-dependent inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.

4. The role of zinc in alcohol dehydrogenases. II. The kinetics of the instantaneous reversible inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.

5. Kinetic studies on the rôle of zinc and diphosphopyridine nucleotide in the activity of yeast alcohol dehydrogenase.

6. Analysis of metal-protein complexes.

Review 7. Aspects of enzyme mechanisms studies by nuclear spin relazation induced by paramagnetic probes.

Review 1. The molecular mechanistic and immunological properties of amine oxidases.

2. Metabolic regulation in C4 photosynthesis: PEP-carboxylase and energy charge.

3. The amine oxidases of human placenta and pregnancy plasma.

4. Correlation of the effects of citric acid cycle metabolites on succinate oxidation by rat liver mitochondria and submitochondrial particles.

5. The glycoprotein nature of pig kidney diamine oxidase. Role of disulphide groups and arginine residues in the concanavalin A-diamine oxidase interaction.

6. Inhibition of enzymes by metal ion-chelating reagents. The action of copper-chelating reagents on diamine oxidase.

7. Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase.