Literature DB >> 4989042

Reversible inhibition in bimolecular rapid equilibrium random order enzyme systems. The effect of substrate-substrate and inhibitor-substrate interactions.

A G Clark.   

Abstract

A model is presented that accounts for all types of reversible inhibition by a single inhibitor molecule in bimolecular rapid-equilibrium random-order enzyme systems. The characterization of inhibition mechanisms by graphical methods is examined, and a system of nomenclature is suggested.

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Year:  1970        PMID： 4989042      PMCID： PMC1179061          DOI： 10.1042/bj1170997

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


  9 in total

1.  TREATMENT OF ENZYME KINETIC DATA. I. THE EFFECT OF MODIFIERS ON THE KINETIC PARAMETERS OF SINGLE SUBSTRATE ENZYMERS.

Authors:  C FRIEDEN
Journal:  J Biol Chem       Date:  1964-10       Impact factor: 5.157

2.  The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory.

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

3.  Graphical determination of the dissociation constants for two-substrate enzyme systems.

Authors:  J R FLORINI; C S VESTLING
Journal:  Biochim Biophys Acta       Date:  1957-09

4.  Graphical analysis of single enzyme systems.

Authors:  B H HOFSTEE
Journal:  Enzymologia       Date:  1956-07-15

5.  The determination of enzyme inhibitor constants.

Authors:  M DIXON
Journal:  Biochem J       Date:  1953-08       Impact factor: 3.857

6.  Enzymes catalysing conjugations of glutathione with alpha-beta-unsaturated carbonyl compounds.

Authors:  E Boyland; L F Chasseaud
Journal:  Biochem J       Date:  1968-10       Impact factor: 3.857

7.  Comparative detoxication. 10. The enzymic conjugation of chloro compounds with glutathione in locusts and other insects.

Authors:  A J Cohen; J N Smith; H Turbert
Journal:  Biochem J       Date:  1964-03       Impact factor: 3.857

8.  The inhibition of 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) dehydrochlorinase and glutathione S-aryltransferase in grass-grub and housefly preparations.

Authors:  S Balabaskaran; J N Smith
Journal:  Biochem J       Date:  1970-05       Impact factor: 3.857

9.  Species differences in the inhibition of glutathione S-aryltransferase by phthaleins and dicarboxylic acids.

Authors:  A G Clark; F J Darby; J N Smith
Journal:  Biochem J       Date:  1967-04       Impact factor: 3.857
  9 in total
  3 in total

1.  Suppression of high-affinity ligand binding to the major glutathione S-transferase from Galleria mellonella by physiological concentrations of glutathione.

Authors:  A G Clark; N Carrol
Journal:  Biochem J       Date:  1986-01-15       Impact factor: 3.857

2.  The inhibition of 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) dehydrochlorinase and glutathione S-aryltransferase in grass-grub and housefly preparations.

Authors:  S Balabaskaran; J N Smith
Journal:  Biochem J       Date:  1970-05       Impact factor: 3.857

3.  Cerebral-cortex hexokinase. Elucidation of reaction mechanisms by substrate and dead-end inhibitor kinetic analysis.

Authors:  H S Bachelard; A G Clark; M F Thompson
Journal:  Biochem J       Date:  1971-08       Impact factor: 3.857
  3 in total

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