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Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae
Author(s) -
Prip-Buus Carina,
Cohen Isabelle,
Kohl Claude,
Esser Victoria,
McGarry J.Denis,
Girard Jean
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00584-5
Subject(s) - saccharomyces cerevisiae , carnitine palmitoyltransferase i , carnitine o palmitoyltransferase , biochemistry , carnitine , mitochondrion , enzyme , yeast , function (biology) , chemistry , biology , kinetics , microbiology and biotechnology , beta oxidation , physics , quantum mechanics
The rat liver carnitine palmitoyltransferase 1 (L‐CPT 1) expressed in Saccharomyces cerevisiae was correctly inserted into the outer mitochondrial membrane and shared the same folded conformation as the native enzyme found in rat liver mitochondria. Comparison of the biochemical properties of the yeast‐expressed L‐CPT 1 with those of the native protein revealed the same detergent lability and similar sensitivity to malonyl‐CoA inhibition and affinity for carnitine. Normal Michaelis‐Menten kinetics towards palmitoyl‐CoA were observed when careful experimental conditions were used for the CPT assay. Thus, the expression in S. cerevisiae is a valid model to study the structure‐function relationships of L‐CPT 1.