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Journal of Lipid Research, Vol. 47, 700-704, April 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

Short Communication

Identification of mouse palmitoyl-coenzyme A 9-desaturase

Makoto Miyazaki^1,*, Sean M. Bruggink^* and James M. Ntambi^1,*,

^* Department of Biochemistry, University of Wisconsin, Madison, WI 53706
Department of Nutritional Sciences, University of Wisconsin, Madison, WI 53706

Published, JLR Papers in Press, February 1, 2006.

¹ To whom correspondence should be addressed. e-mail: miyazakim{at}biochem.wisc.edu (M.M.); ntambi{at}biochem.wisc.edu (J.M.N.)

ABSTRACT

Stearoyl-coenzyme A desaturase (SCD) catalyzes the desaturation of saturated fatty acids to monounsaturated fatty acids in mammalian cells. Currently, there are four known enzymatic isoforms (SCD1–SCD4) in the mouse genome. The physiological roles for multiple SCD isoforms and their substrate specificities are unknown at present. We report here distinct substrate specificities for the mouse SCD isoforms. Each SCD isoform was able to complement the ole1 mutation in Saccharomyces cerevisiae through heterologous expression of transgenic SCD. Fatty acid analysis showed that mouse SCD1, SCD2, and SCD4 desaturate both C18:0 and C16:0, whereas mouse SCD3 uses C16:0 but not C18:0. We identify SCD3 as a mammalian palmitotyl-CoA 9-desaturase, and its existence in mouse helps explain distinct physiological roles for each SCD isoform.

Supplementary key words stearoyl-CoA desaturase • oleate • palmitoleate • substrate specificity

Abbreviations: PCD, palmitoyl-coenzyme A 9-desaturase; SCD, stearoyl-coenzyme A desaturase

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