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- W2008075253 abstract "The outer mitochondrial membrane enzyme carnitine palmitoyltransferase I (CPTI) catalyzes the initial and regulatory step in the β-oxidation of fatty acids. The genes for the two isoforms of CPTI-liver (L-CPTI) and muscle (M-CPTI) have been cloned and expressed, and the genes encode for enzymes with very different kinetic properties and sensitivity to malonyl-CoA inhibition. Pig L-CPTI encodes for a 772 amino acid protein that shares 86 and 62% identity, respectively, with rat L- and M-CPTI. When expressed in Pichia pastoris, the pig L-CPTI enzyme shows kinetic characteristics (carnitine, Km = 126 μM; palmitoyl-CoA, Km = 35 μM) similar to human or rat L-CPTI. However, the pig enzyme, unlike the rat liver enzyme, shows a much higher sensitivity to malonyl-CoA inhibition (IC50 = 141 nM) that is characteristic of human or rat M-CPTI enzymes. Therefore, pig L-CPTI behaves like a natural chimera of the L- and M-CPTI isotypes, which makes it a useful model to study the structure−function relationships of the CPTI enzymes." @default.
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- W2008075253 date "2001-01-26" @default.
- W2008075253 modified "2023-09-27" @default.
- W2008075253 title "Pig Liver Carnitine Palmitoyltransferase I, with Low <i>K</i><sub>m</sub> for Carnitine and High Sensitivity to Malonyl-CoA Inhibition, Is a Natural Chimera of Rat Liver and Muscle Enzymes" @default.
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- W2008075253 doi "https://doi.org/10.1021/bi0024106" @default.
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