Purification and some kinetic properties of rat liver ATP citrate lyase

Biochem J. 1984 Dec 1;224(2):437-43. doi: 10.1042/bj2240437.

Abstract

A new purification procedure for rat liver ATP citrate lyase is described. The method reproducibly gives homogenous undegraded enzyme. Steady-state kinetic analysis of ATP citrate lyase was complicated by the presence of ADP, a product of the reaction, in solutions of ATP. The kinetic patterns observed were dependent on whether ADP was removed by the assay system. When assays were performed with a method in which ADP was removed, the results showed that the enzyme obeys a double-displacement mechanism with a phosphoenzyme intermediate. This resolves a controversy between the results of previous kinetic studies and those of isotope-exchange and enzyme-labelling experiments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP Citrate (pro-S)-Lyase / isolation & purification
  • ATP Citrate (pro-S)-Lyase / metabolism*
  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Animals
  • Citrates / metabolism
  • Citric Acid
  • Coenzyme A / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Kinetics
  • Liver / enzymology*
  • Male
  • Rats
  • Rats, Inbred Strains

Substances

  • Citrates
  • Citric Acid
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • ATP Citrate (pro-S)-Lyase
  • Coenzyme A