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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Carnitine O-Palmitoyltransferase / chemistry
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Carnitine O-Palmitoyltransferase / deficiency*
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Carnitine O-Palmitoyltransferase / physiology
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Cell Membrane / enzymology
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Chromosomes, Human, Pair 1 / genetics
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Computer Simulation
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DNA Mutational Analysis
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Helix-Turn-Helix Motifs
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Humans
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Lipid Bilayers / chemistry
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Lipid Metabolism, Inborn Errors / enzymology
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Lipid Metabolism, Inborn Errors / genetics*
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Models, Molecular
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Molecular Sequence Data
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Mutation, Missense
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Myoglobinuria / enzymology
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Myoglobinuria / genetics*
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Point Mutation
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Protein Conformation
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Protein Structure, Tertiary
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Rhabdomyolysis / enzymology
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Rhabdomyolysis / genetics*
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Sequence Alignment
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Sequence Deletion
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Sequence Homology, Amino Acid
Substances
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Lipid Bilayers
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Carnitine O-Palmitoyltransferase