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Title: Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the enzyme are important for the unusual high malonyl-CoA sensitivity
Author: Nicot, Carine
Relat Pardo, Joana
Woldegiorgis, Gebre
Haro Bautista, Diego
Marrero González, Pedro F.
Keywords: Carnitina palmitoïl-transferasa 1
Cinètica enzimàtica
Carnitine palmitoyltransferase I
Enzyme kinetics
Amino acids
Issue Date: Mar-2002
Publisher: American Society for Biochemistry and Molecular Biology
Abstract: Pig and rat liver carnitine palmitoyltransferase I (L-CPTI) share common K(m) values for palmitoyl-CoA and carnitine. However, they differ widely in their sensitivity to malonyl-CoA inhibition. Thus, pig l-CPTI has an IC(50) for malonyl-CoA of 141 nm, while that of rat L-CPTI is 2 microm. Using chimeras between rat L-CPTI and pig L-CPTI, we show that the entire C-terminal region behaves as a single domain, which dictates the overall malonyl-CoA sensitivity of this enzyme. The degree of malonyl-CoA sensitivity is determined by the structure adopted by this domain. Using deletion mutation analysis, we show that malonyl-CoA sensitivity also depends on the interaction of this single domain with the first 18 N-terminal amino acid residues. We conclude that pig and rat L-CPTI have different malonyl-CoA sensitivity, because the first 18 N-terminal amino acid residues interact differently with the C-terminal domain. This is the first study that describes how interactions between the C- and N-terminal regions can determine the malonyl-CoA sensitivity of L-CPTI enzymes using active C-terminal chimeras.
Note: Reproducció del document publicat a:
It is part of: Journal of Biological Chemistry, 2002, vol. 277, num. 12, p. 10044-10049
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ISSN: 0021-9258
Appears in Collections:Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia)

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