Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae

FEBS Lett. 1998 Jun 12;429(2):173-8. doi: 10.1016/s0014-5793(98)00584-5.


The rat liver carnitine palmitoyltransferase 1 (L-CPT 1) expressed in Saccharomyces cerevisiae was correctly inserted into the outer mitochondrial membrane and shared the same folded conformation as the native enzyme found in rat liver mitochondria. Comparison of the biochemical properties of the yeast-expressed L-CPT 1 with those of the native protein revealed the same detergent lability and similar sensitivity to malonyl-CoA inhibition and affinity for carnitine. Normal Michaelis-Menten kinetics towards palmitoyl-CoA were observed when careful experimental conditions were used for the CPT assay. Thus, the expression in S. cerevisiae is a valid model to study the structure-function relationships of L-CPT 1.

Publication types

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

MeSH terms

  • Animals
  • Carnitine / metabolism
  • Carnitine O-Palmitoyltransferase / chemistry
  • Carnitine O-Palmitoyltransferase / genetics
  • Carnitine O-Palmitoyltransferase / metabolism*
  • Mitochondria / enzymology
  • Mitochondria, Liver / enzymology*
  • Palmitoyl Coenzyme A / metabolism
  • Rabbits
  • Rats
  • Rats, Wistar
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Subcellular Fractions
  • Substrate Specificity


  • Recombinant Fusion Proteins
  • Palmitoyl Coenzyme A
  • Carnitine O-Palmitoyltransferase
  • Carnitine