New insights into the mitochondrial carnitine palmitoyltransferase enzyme system

J. D. McGarry, A. Sen, V. Esser, K. F. Woeltje, B. Weis, D. W. Foster

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

Dissection of the mitochondrial carnitine palmitoyltransferase (CPT) enzyme system in terms of its structure/function relationships has proved to be a formidable task. Although no one formulation has gained universal agreement we believe that the weight of evidence supports a model with the following features: a) in any given tissue CPT I and CPT II are distinct proteins: b) CPT I, unlike CPT II, is detergent labile: c) within a species CPT II is expressed body wide, whereas CPT I exists as tissue specific isoforms; d) malonyl-CoA and other CPT I inhibitors probably interact at the catalytic center of the enzyme, not with a regulatory subunit. The amino acid sequences of rat and human CPT II (deduced from cDNA clones) show them to be similar proteins (> 80% identity) but encoded by mRNAs of significantly different sizes. Efforts to clone and sequence the cDNA for rat liver CPT I are presently underway.

Original languageEnglish (US)
Pages (from-to)77-84
Number of pages8
JournalBiochimie
Volume73
Issue number1
DOIs
StatePublished - Jan 1991

Keywords

  • carnitine palmitoyltransferase
  • isoforms
  • structure/function

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'New insights into the mitochondrial carnitine palmitoyltransferase enzyme system'. Together they form a unique fingerprint.

  • Cite this