Carnitine palmitoyltransferase II deficiency: molecular and biochemical analysis of 32 patients

Neurology. 2003 Apr 22;60(8):1351-3. doi: 10.1212/01.wnl.0000055901.58642.48.

Abstract

The authors investigated 32 patients with the muscle form of CPT II deficiency. Total carnitine palmitoyltransferase enzyme system (CPT) activity was normal but abnormally inhibited by malonyl-CoA, palmitoyl-CoA, and the detergents Triton X and Tween 20. Mutation analysis identified three described mutations (S113L, P50H, and F448L) and two novel mutations (M214T and Y479F). Using modeling techniques, a structure could be identified anchoring the protein in the membrane. Only one of the five mutations (Y479F) is located within this region.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Carnitine O-Palmitoyltransferase / chemistry
  • Carnitine O-Palmitoyltransferase / deficiency*
  • Carnitine O-Palmitoyltransferase / physiology
  • Cell Membrane / enzymology
  • Chromosomes, Human, Pair 1 / genetics
  • Computer Simulation
  • DNA Mutational Analysis
  • Helix-Turn-Helix Motifs
  • Humans
  • Lipid Bilayers / chemistry
  • Lipid Metabolism, Inborn Errors / enzymology
  • Lipid Metabolism, Inborn Errors / genetics*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation, Missense
  • Myoglobinuria / enzymology
  • Myoglobinuria / genetics*
  • Point Mutation
  • Protein Conformation
  • Protein Structure, Tertiary
  • Rhabdomyolysis / enzymology
  • Rhabdomyolysis / genetics*
  • Sequence Alignment
  • Sequence Deletion
  • Sequence Homology, Amino Acid

Substances

  • Lipid Bilayers
  • Carnitine O-Palmitoyltransferase