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J. Biol. Chem., Vol. 269, Issue 42, 26438-26442, Oct, 1994
NF Brown, V Esser, DW Foster and JD McGarry
A cDNA encoding full-length carnitine palmitoyltransferase I (CPT I) from
rat liver was expressed in Saccharomyces cerevisiae, a system devoid of
endogenous CPT activity. The recombinant enzyme was of the expected size
(as deduced from immunoblots), membrane-bound, and detergent-labile. It was
also potently inhibited by malonyl-CoA, with an I50 value (concentration
causing 50% inhibition) of approximately 5 microM, similar to that of the
native enzyme in rat liver mitochondria. A truncated variant of the enzyme
that lacked the amino-terminal 82 residues encompassing the first
hydrophobic domain retained catalytic function but was much less sensitive
to malonyl-CoA (I50 > 80 microM). Deletion of the cDNA segment encoding
amino acids 31-148 (which includes both first and second hydrophobic
stretches) resulted in no detectable product. The data establish
unequivocally that a single polypeptide possesses both catalytic and
malonyl-CoA binding domains, as well as the other properties previously
attributed by us to native CPT I in mammalian mitochondria, and should thus
put to rest the controversy surrounding this issue (Kerner, J., Zaluzec,
E., Gage, D., and Bieber, L. L. (1994) J. Biol. Chem. 269, 8209-8219). In
addition, the results strengthen the view that one site of interaction of
malonyl- CoA with the rat liver enzyme involves the NH2-terminal region of
the molecule.
Expression of a cDNA for rat liver carnitine palmitoyltransferase I in yeast establishes that catalytic activity and malonyl-CoA sensitivity reside in a single polypeptide
Department of Internal Medicine, University of Texas Southwestern Medical Center, Southwestern Medical School, Dallas 75235.
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