Identification of mouse palmitoyl-coenzyme A Delta9-desaturase.
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 Delta9-desaturase, and its existence in mouse helps explain distinct physiological roles for each SCD isoform.
Miyazaki
Makoto
M
Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA. miyazakim@biochem.wisc.edu
Bruggink
Sean M
SM
Ntambi
James M
JM
D000818:Animals; D044943:Fatty Acid Desaturases / Q000235:genetics / Q000378:metabolism*; D005227:Fatty Acids / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D019076:Transgenes
D005227:Fatty Acids; D007527:Isoenzymes; D044943:Fatty Acid Desaturases; C022311:palmitoyl-CoA desaturase