Intraorganellar localization of CoASH-independent phytanic acid oxidation in human liver peroxisomes

FEBS Lett. 1993 Oct 25;333(1-2):154-8. doi: 10.1016/0014-5793(93)80395-b.


In human tissues phytanic acid is alpha-oxidized to pristanic acid in peroxisomes. Studies of the intraorganellar site of alpha-oxidation of [1-14C]phytanic acid to pristanic acid in peroxisomes isolated from human liver demonstrate that phytanoyl-CoA ligase is present in the peroxisomal membrane and that the enzyme system for alpha-oxidation of phytanic acid to pristanic acid is in the peroxisomal matrix. In contrast to the beta-oxidation system for fatty acids, the substrate for alpha-oxidation is free phytanic acid. The studies described in this manuscript report a novel fatty acid oxidation system where the substrate for the enzyme system is free fatty acid; however, phytanoyl-CoA ligase regulates the alpha-oxidation of phytanic acid at the organellar (peroxisomal) level.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Coenzyme A / metabolism*
  • Coenzyme A Ligases / metabolism
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Liver / metabolism*
  • Microbodies / metabolism*
  • Oxidation-Reduction
  • Phytanic Acid / metabolism*


  • Phytanic Acid
  • Coenzyme A Ligases
  • phytanoyl-CoA ligase
  • Coenzyme A