Literature DB >> 200838

Uridine-cytidine kinase. III. Competition between uridine and cytidine for a single enzyme.

A S Liacouras, E P Anderson.   

Abstract

The combined phosphorylation of uridine and cytidine by a partially purified preparation of uridine-cytidine kinase has been studied with dual-substrate kinetics. The kinetic patterns obtained are consistent with the theoretical analysis for two competing, alternate substrates interacting with a single enzyme. Thus, despite feedback regulation of the kinase by both UTP and CTP, the results allow a clear conclusion that both nucleosides are phosphorylated by the same enzyme, and probably at a single site, rather than by two closely related isozymes, each specific for one pyrimidine.

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Year:  1977        PMID: 200838     DOI: 10.1007/bf01730833

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  14 in total

1.  Inhibition and activation of adenylosuccinic synthetase by 8-azaguanosine triphosphate.

Authors:  L H COHEN; R E PARKS
Journal:  Can J Biochem Physiol       Date:  1963-07

2.  Computer programmes for processing enzyme kinetic data.

Authors:  W W CLELAND
Journal:  Nature       Date:  1963-05-04       Impact factor: 49.962

3.  A theoretical basis of molecular pharmacology. I. Interactions of one or two compounds with one receptor system.

Authors:  E J ARIENS; J M VAN ROSSUM; A M SIMONIS
Journal:  Arzneimittelforschung       Date:  1956-05

4.  Uridine-cytidine kinase. Kinetic studies and reaction mechanism.

Authors:  A S Liacouras; T Q Garvey; F K Millar; E P Anderson
Journal:  Arch Biochem Biophys       Date:  1975-05       Impact factor: 4.013

5.  A method for determining the ratio of the Michaelis constants of an enzyme with respect to two substrates.

Authors:  M B THORN
Journal:  Nature       Date:  1949-07-02       Impact factor: 49.962

6.  Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds and endogenous substrates. V. Competition between cytochromes P-450 and P-448 for reductase in 3,4-benzpyrene hydroxylation.

Authors:  S B West; A Y Lu
Journal:  Arch Biochem Biophys       Date:  1972-11       Impact factor: 4.013

7.  Two-substrate kinetics of drug-metabolizing enzyme systems of hepatic microsomes.

Authors:  A P Alvares; G J Mannering
Journal:  Mol Pharmacol       Date:  1970-05       Impact factor: 4.436

8.  Induction of drug metabolism. II. Qualitative differences in the microsomal N-demethylating systems stimulated by polycyclic hydrocarbons and by phenobarbital.

Authors:  N E Sladek; G J Mannering
Journal:  Mol Pharmacol       Date:  1969-03       Impact factor: 4.436

9.  Kinetics of enzyme reactions with competing alternative substrates.

Authors:  S Cha
Journal:  Mol Pharmacol       Date:  1968-11       Impact factor: 4.436

10.  Competition of two substrates for a single enzyme. A simple kinetic theorem exemplified by a hydroxy steroid dehydrogenase reaction.

Authors:  T Pocklington; J Jeffery
Journal:  Biochem J       Date:  1969-04       Impact factor: 3.857

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