Adenosine triphosphate conservation in metabolic regulation: rat liver citrate cleavage enzyme
DE Atkinson, GM Walton - Journal of Biological Chemistry, 1967 - ASBMB
The citrate cleavage enzyme (EC 4.1. 3.8) of rat liver is inhibited by adenosine diphosphate,
which appears to compete with adenosine triphosphate. This effect may ensure that fatty
acids are produced only when the ATP level is high. The" energy charge" of the adenylate
system, defined as (ATP+ ½ ADP)/(AMP+ ADP+ ATP), is proposed as a fundamental
metabolic control parameter. Enzymes that utilize ATP and are inhibited by ADP or AMP will
yield steep curves of velocity as a function of energy charge (resembling the steep curves of …
which appears to compete with adenosine triphosphate. This effect may ensure that fatty
acids are produced only when the ATP level is high. The" energy charge" of the adenylate
system, defined as (ATP+ ½ ADP)/(AMP+ ADP+ ATP), is proposed as a fundamental
metabolic control parameter. Enzymes that utilize ATP and are inhibited by ADP or AMP will
yield steep curves of velocity as a function of energy charge (resembling the steep curves of …