Carnitine palmitoyltransferase II deficiency: molecular and biochemical analysis of 32 patients.
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.
Wieser
T
T
Klinik und Poliklinik für Neurologie, Martin-Luther-Universität, Halle/Saale, Germany. thomas.wieser@medizin.uni-halle.de
Deschauer
M
M
Olek
K
K
Hermann
T
T
Zierz
S
S
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002334:Carnitine O-Palmitoyltransferase / Q000737:chemistry / Q000172:deficiency* / Q000502:physiology; D002462:Cell Membrane / Q000201:enzymology; D002878:Chromosomes, Human, Pair 1 / Q000235:genetics; D003198:Computer Simulation; D004252:DNA Mutational Analysis; D019077:Helix-Turn-Helix Motifs; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry; D008052:Lipid Metabolism, Inborn Errors / Q000201:enzymology / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020125:Mutation, Missense; D009212:Myoglobinuria / Q000201:enzymology / Q000235:genetics*; D017354:Point Mutation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012206:Rhabdomyolysis / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D008051:Lipid Bilayers; D002334:Carnitine O-Palmitoyltransferase