Coenzyme A metabolism

Am J Physiol. 1985 Jan;248(1 Pt 1):E1-9. doi: 10.1152/ajpendo.1985.248.1.E1.


The metabolism of coenzyme A and control of its synthesis are reviewed. Pantothenate kinase is an important rate-controlling enzyme in the synthetic pathway of all tissues studied and appears to catalyze the flux-generating reaction of the pathway in cardiac muscle. This enzyme is strongly inhibited by coenzyme A and all of its acyl esters. The cytosolic concentrations of coenzyme A and acetyl coenzyme A in both liver and heart are high enough to totally inhibit pantothenate kinase under all conditions. Free carnitine, but not acetyl carnitine, deinhibits the coenzyme A-inhibited enzyme. Carnitine alone does not increase enzyme activity. Thus changes in the acetyl carnitine-to-carnitine ratio that occur with nutritional states provides a mechanism for regulation of coenzyme A synthetic rates. Changes in the rate of coenzyme A synthesis in liver and heart occurs with fasting, refeeding, and diabetes and in heart muscle with hypertrophy. The pathway and regulation of coenzyme A degradation are not understood.

Publication types

  • Review

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Animals
  • Coenzyme A / biosynthesis
  • Coenzyme A / metabolism*
  • Diet
  • Kinetics
  • Liver / metabolism
  • Myocardium / metabolism
  • Pantothenic Acid / metabolism
  • Phosphotransferases (Alcohol Group Acceptor)*
  • Phosphotransferases / metabolism
  • Subcellular Fractions / metabolism
  • Tissue Distribution


  • Pantothenic Acid
  • Acetyl Coenzyme A
  • Phosphotransferases
  • Phosphotransferases (Alcohol Group Acceptor)
  • pantothenate kinase
  • Coenzyme A