J. Lipid Res.
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A more recent version of this article appeared on April 1, 2006 Originally published In Press as doi:10.1194/jlr.C500025-JLR200 on January 27, 2006

Papers In Press, published online ahead of print February 1, 2006
J. Lipid Res., doi:10.1194/jlr.C500025-JLR200
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Submitted on December 16, 2005
Revised on January 25, 2006
Accepted on January 25, 2006

Identification of mouse palmitoyl-CoA Delta 9 desaturase

Makoto Miyazaki, Sean M. Bruggink, and James M. Ntambi

Biochemsitry Dept., University of Wisconsin-Madison, Madison, WI 53706

Corresponding Author: ntambi{at}biochem.wisc.edu

Stearoyl-CoA desaturase (SCD) catalyzes the desaturation of saturated fatty acids to monounsaturated fatty acids in mammalian cells. Currently, there are four known enzymatic isoforms (SCD1-4) in mouse genome. The physiological role for multiple SCD isoforms and their substrate specificities are currently unknown. We report here distinct substrate specificities for the mouse SCD isoforms. Each SCD isoform was able to complement the OLE-1 mutation in S. 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 utilizes C16:0 but not C18:0. We identify SCD3 as a mammalian palmitotyl-CoA Delta 9 desaturase and its existence in mouse helps to explain distinct physiological roles for each SCD isoform.


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