Identification of mouse palmitoyl-coenzyme A Δ9-desaturase

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 Δ9-desaturase, and its existence in mouse helps explain distinct physiological roles for each SCD isoform. 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 Δ9-desaturase, and its existence in mouse helps explain distinct physiological roles for each SCD isoform. Δ9-desaturase is a fatty acid-modifying enzyme in the biosynthesis of monounsaturated fatty acids. Because this enzyme commonly introduces a cis double bond at the 9,10 position of stearoyl-CoA to form oleoyl-CoA, it has been commonly known as stearoyl-coenzyme A desaturase (SCD) (1Miyazaki M. Ntambi J.M. Role of stearoyl-coenzyme A desaturase in lipid metabolism.Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 113-121Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar, 2Ntambi J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar, 3Shanklin J. Whittle E. Fox B.G. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase.Biochemistry. 1994; 33: 12787-12794Crossref PubMed Scopus (644) Google Scholar, 4Fox B.G. Shanklin J. Somerville C. Munck E. Stearoyl-acyl carrier protein delta 9 desaturase from Ricinus communis is a diiron-oxo protein.Proc. Natl. Acad. Sci. USA. 1993; 90: 2486-2490Crossref PubMed Scopus (239) Google Scholar, 5Ntambi J.M. Regulation of stearoyl-CoA desaturase by polyunsaturated fatty acids and cholesterol.J. Lipid Res. 1999; 40: 1549-1558Abstract Full Text Full Text PDF PubMed Google Scholar). Four SCD isoforms (SCD1–SCD4) been in Ntambi J.M. expression in A stearoyl-CoA Full Text PDF PubMed Google Scholar, M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, J.M. E. expression in of a stearoyl-CoA Full Text PDF PubMed Google Scholar, of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). mouse SCD are to of the stearoyl-CoA desaturase expression in PubMed Scopus Google the that the four SCD isoforms and acid in their in expression J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar). is in and J.M. E. expression in of a stearoyl-CoA Full Text PDF PubMed Google Scholar). is in the and the Ntambi J.M. expression in A stearoyl-CoA Full Text PDF PubMed Google Scholar). SCD3 expression is to in and of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar, M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google Scholar, M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar). SCD4 is in M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). and are the isoforms of the of and and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, M. Ntambi J.M. expression is for lipid and Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). a in the of and a are and but and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, Miyazaki M. Ntambi J.M. J.M. Role for stearoyl-CoA in PubMed Scopus Google Scholar, J.M. Miyazaki M. J.M. of stearoyl-CoA Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). a in and a in the of but not at of M. Ntambi J.M. expression is for lipid and Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). that is in lipid in it is unknown multiple SCD isoforms in mammalian the expression and the of and mouse isoform that each isoform has a distinct physiological it is not the the roles from and a in the of both and to and that and and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, M. Ntambi J.M. expression is for lipid and Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). from the of SCD the of M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google the existence of Δ9-desaturase in the of each isoform at the position of saturated it is that both and fatty acids as the physiological of each mouse SCD substrate to isoform for and We in this that SCD1, SCD2, and SCD4 both and saturated SCD3 but not of mouse SCD of mouse SCD isoforms by mouse as and a of and a enzyme and a and a enzyme The was into a expression M. for the expression of heterologous in PubMed Scopus Google a mammalian expression the mouse into Saccharomyces cerevisiae The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google by a of the Δ9-desaturase the A and for of Google Scholar). cerevisiae fatty acids for The a and acid but the of the fatty acids. at for at in a in and The in and and of was to a of of the mouse SCD was into cells. was to the in the and The was to a of a of The to in at for and SCD acid in fatty acids for and by in of in The was to for and Fatty acids to and A of lipid and J. PubMed Scopus Google and of in The fatty acid and by M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, J. A fatty acid desaturase from Res. PubMed Scopus Google Scholar, A 9 fatty acid desaturase from the 2003; PubMed Scopus Google Scholar). saturated fatty acids into in the of The double bond of the monounsaturated fatty acid by analysis of the M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar, of double bond position in by of Scopus Google from by and in a Δ9-desaturase was at for and of protein M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google protein was by and to a The was at for in and at in for the was a of for at The was the are as was to the of mouse SCD the of the in the expression the The was to a Δ9-desaturase in each SCD able to fatty that the mouse in by their to complement the ole1 The fatty acid of as by are in and fatty acid and and of to and and of to of and of but the of and the mouse SCD1, SCD2, and SCD4 desaturate and to and the SCD3 of to but the of to was that this isoform C16:0 as a analysis a showed that Δ9-desaturase in at the The of the double bond in monounsaturated fatty acids by analysis of the the of and in SCD showed the at and not acid of in acid of of stearoyl-coenzyme A the of each fatty acid in of fatty acids of the and are for in a the mouse SCD isoforms desaturate saturated fatty the saturated fatty acids to each SCD isoform and and of to and of to and of to and and of to of of and of to and The of to was in SCD4 of and of that as of the SCD isoforms a saturated fatty of saturated fatty acids to monounsaturated fatty acids. Fatty acids in the of and for the mouse substrate specificities in mammalian the into a mammalian expression and into Δ9-desaturase and not and as and are the monounsaturated fatty acids in mammalian cells. The substrate of of the in mammalian are in and and but and Δ9-desaturase showed but its was not in mouse in the of Each the are four known Δ9-desaturase isoforms in mouse that are for the biosynthesis of monounsaturated fatty and J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar). for The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google the substrate specificities of mammalian not been in the for the existence and expression of the multiple isoforms a that fatty acids for and of that mouse SCD isoforms substrate the from both and are of and there was SCD4 both and but the was of isoforms. the of SCD4 SCD3 uses C16:0 but not C18:0. this SCD3 A substrate of protein Δ9-desaturase has been of the of the Shanklin J. J. A of substrate from the carrier protein desaturase of PubMed Scopus Google Scholar). and the at position was to the of Δ9-desaturase Shanklin J. J. A of substrate from the carrier protein desaturase of PubMed Scopus Google Scholar). of the in the the histidine and the are conserved in the mouse the distinct substrate the of mouse and are M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). The acid are in acid residues the histidine that acid in this of the protein as a of their are to this the for the existence of and its to monounsaturated fatty acids is it to the of the SCD and the in of their monounsaturated fatty acid is in lipid to as of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). The monounsaturated fatty acid in is in fatty acid Full Text PDF PubMed Scopus Google Scholar). Because is is by the The of is that of to to and by and M. of of the Full Text Full Text PDF PubMed Scopus Google in the of The of of the and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, is in and is in the 1999; PubMed Scopus Google Scholar). expression was in of of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar, M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar). that from is fatty acid in the of and that of SCD and the in the of and its in the of is that of and its M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google Scholar). that the desaturase in the of is that of Δ9-desaturase is a fatty acid-modifying enzyme in the biosynthesis of monounsaturated fatty acids. Because this enzyme commonly introduces a cis double bond at the 9,10 position of stearoyl-CoA to form oleoyl-CoA, it has been commonly known as stearoyl-coenzyme A desaturase (SCD) (1Miyazaki M. Ntambi J.M. Role of stearoyl-coenzyme A desaturase in lipid metabolism.Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 113-121Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar, 2Ntambi J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar, 3Shanklin J. Whittle E. Fox B.G. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase.Biochemistry. 1994; 33: 12787-12794Crossref PubMed Scopus (644) Google Scholar, 4Fox B.G. Shanklin J. Somerville C. Munck E. Stearoyl-acyl carrier protein delta 9 desaturase from Ricinus communis is a diiron-oxo protein.Proc. Natl. Acad. Sci. USA. 1993; 90: 2486-2490Crossref PubMed Scopus (239) Google Scholar, 5Ntambi J.M. Regulation of stearoyl-CoA desaturase by polyunsaturated fatty acids and cholesterol.J. Lipid Res. 1999; 40: 1549-1558Abstract Full Text Full Text PDF PubMed Google Scholar). Four SCD isoforms (SCD1–SCD4) been in Ntambi J.M. expression in A stearoyl-CoA Full Text PDF PubMed Google Scholar, M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, J.M. E. expression in of a stearoyl-CoA Full Text PDF PubMed Google Scholar, of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). mouse SCD are to of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). the that the four SCD isoforms and acid in their in expression J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar). is in and J.M. E. expression in of a stearoyl-CoA Full Text PDF PubMed Google Scholar). is in the and the Ntambi J.M. expression in A stearoyl-CoA Full Text PDF PubMed Google Scholar). SCD3 expression is to in and of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar, M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google Scholar, M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar). SCD4 is in M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). and are the isoforms of the of and and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, M. Ntambi J.M. expression is for lipid and Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). a in the of and a are and but and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, Miyazaki M. Ntambi J.M. J.M. Role for stearoyl-CoA in PubMed Scopus Google Scholar, J.M. Miyazaki M. J.M. of stearoyl-CoA Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). a in and a in the of but not at of M. Ntambi J.M. expression is for lipid and Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). that is in lipid in Currently, it is unknown multiple SCD isoforms in mammalian the expression and the of and mouse isoform that each isoform has a distinct physiological it is not the the roles from and a in the of both and to and that and and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, M. Ntambi J.M. expression is for lipid and Natl. Acad. Sci. USA. PubMed Scopus Google Scholar). from the of SCD the of M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google the existence of Δ9-desaturase in the of each isoform at the position of saturated it is that both and fatty acids as the physiological of each mouse SCD substrate to isoform for and We in this that SCD1, SCD2, and SCD4 both and saturated SCD3 but not of mouse SCD of mouse SCD isoforms by mouse as and a of and a enzyme and a and a enzyme The was into a expression M. for the expression of heterologous in PubMed Scopus Google a mammalian expression the mouse into Saccharomyces cerevisiae The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google by a of the Δ9-desaturase the A and for of Google Scholar). cerevisiae fatty acids for The a and acid but the of the fatty acids. at for at in a in and The in and and of was to a of of the mouse SCD was into cells. was to the in the and The was to a of a of The to in at for and SCD acid in fatty acids for and by in of in The was to for and Fatty acids to and A of lipid and J. PubMed Scopus Google and of in The fatty acid and by M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, J. A fatty acid desaturase from Res. PubMed Scopus Google Scholar, A 9 fatty acid desaturase from the 2003; PubMed Scopus Google Scholar). saturated fatty acids into in the of The double bond of the monounsaturated fatty acid by analysis of the M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar, of double bond position in by of Scopus Google from by and in a Δ9-desaturase was at for and of protein M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google protein was by and to a The was at for in and at in for the was a of for at The was the are as was to of mouse SCD of mouse SCD isoforms by mouse as and a of and a enzyme and a and a enzyme The was into a expression M. for the expression of heterologous in PubMed Scopus Google a mammalian expression The of mouse SCD isoforms by mouse as and a of and a enzyme and a and a enzyme The was into a expression M. for the expression of heterologous in PubMed Scopus Google a mammalian expression the mouse into Saccharomyces cerevisiae The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google by a of the Δ9-desaturase the A and for of Google Scholar). cerevisiae fatty acids for The a and acid but the of the fatty acids. at for at in a in and The in and and of was to a of of the mouse SCD was into cells. was to the in the and The was to a of a of The to in at for and SCD The the mouse into Saccharomyces cerevisiae The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google by a of the Δ9-desaturase the A and for of Google Scholar). cerevisiae fatty acids for The a and acid but the of the fatty acids. at for at in a in and The in and and of was to a of of the mouse SCD was into cells. was to the in the and The was to a of a of The to in at for and SCD Fatty acid in fatty acids for and by in of in The was to for and Fatty acids to and A of lipid and J. PubMed Scopus Google and of in The fatty acid and by M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, J. A fatty acid desaturase from Res. PubMed Scopus Google Scholar, A 9 fatty acid desaturase from the 2003; PubMed Scopus Google Scholar). saturated fatty acids into in the of The double bond of the monounsaturated fatty acid by analysis of the M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar, of double bond position in by of Scopus Google Scholar). in fatty acids for and by in of in The was to for and Fatty acids to and A of lipid and J. PubMed Scopus Google and of in The fatty acid and by M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, J. A fatty acid desaturase from Res. PubMed Scopus Google Scholar, A 9 fatty acid desaturase from the 2003; PubMed Scopus Google Scholar). saturated fatty acids into in the of The double bond of the monounsaturated fatty acid by analysis of the M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar, of double bond position in by of Scopus Google Scholar). Δ9-desaturase from by and in a Δ9-desaturase was at for and of protein M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar). from by and in a Δ9-desaturase was at for and of protein M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar). protein was by and to a The was at for in and at in for the was a of for at The was the protein was by and to a The was at for in and at in for the was a of for at The was the are as was to are as was to the of mouse SCD the of the in the expression the The was to a Δ9-desaturase in each SCD able to fatty that the mouse in by their to complement the ole1 The fatty acid of as by are in and fatty acid and and of to and and of to of and of but the of and the mouse SCD1, SCD2, and SCD4 desaturate and to and the SCD3 of to but the of to was that this isoform C16:0 as a analysis a showed that Δ9-desaturase in at the The of the double bond in monounsaturated fatty acids by analysis of the the of and in SCD showed the at and not acid of in acid of of stearoyl-coenzyme A the of each fatty acid in of fatty acids of the and are for in a the mouse SCD isoforms desaturate saturated fatty the saturated fatty acids to each SCD isoform and and of to and of to and of to and and of to of of and of to and The of to was in SCD4 of and of that as of the SCD isoforms a saturated fatty the mouse substrate specificities in mammalian the into a mammalian expression and into Δ9-desaturase and not and as and are the monounsaturated fatty acids in mammalian cells. The substrate of of the in mammalian are in and and but and Δ9-desaturase showed but its was not in mouse in the of Each the the of mouse SCD the of the in the expression the The was to a Δ9-desaturase in each SCD able to fatty that the mouse in by their to complement the ole1 The fatty acid of as by are in and fatty acid and and of to and and of to of and of but the of and the mouse SCD1, SCD2, and SCD4 desaturate and to and the SCD3 of to but the of to was that this isoform C16:0 as a analysis a showed that Δ9-desaturase in at the The of the double bond in monounsaturated fatty acids by analysis of the the of and in SCD showed the at and not stearoyl-coenzyme A the of each fatty acid in of fatty acids of the and are for the mouse SCD isoforms desaturate saturated fatty the saturated fatty acids to each SCD isoform and and of to and of to and of to and and of to of of and of to and The of to was in SCD4 of and of that as of the SCD isoforms a saturated fatty the mouse substrate specificities in mammalian the into a mammalian expression and into Δ9-desaturase and not and as and are the monounsaturated fatty acids in mammalian cells. The substrate of of the in mammalian are in and and but and Δ9-desaturase showed but its was not are four known Δ9-desaturase isoforms in mouse that are for the biosynthesis of monounsaturated fatty and J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar). for The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google the substrate specificities of mammalian not been in the for the existence and expression of the multiple isoforms a that fatty acids for and of that mouse SCD isoforms substrate the from both and are of and there was SCD4 both and but the was of isoforms. the of SCD4 SCD3 uses C16:0 but not C18:0. this SCD3 A substrate of protein Δ9-desaturase has been of the of the Shanklin J. J. A of substrate from the carrier protein desaturase of PubMed Scopus Google Scholar). and the at position was to the of Δ9-desaturase Shanklin J. J. A of substrate from the carrier protein desaturase of PubMed Scopus Google Scholar). of the in the the histidine and the are conserved in the mouse the distinct substrate the of mouse and are M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). The acid are in acid residues the histidine that acid in this of the protein as a of their are to this the for the existence of and its to monounsaturated fatty acids is it to the of the SCD and the in of their monounsaturated fatty acid is in lipid to as of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). The monounsaturated fatty acid in is in fatty acid Full Text PDF PubMed Scopus Google Scholar). Because is is by the The of is that of to to and by and M. of of the Full Text Full Text PDF PubMed Scopus Google in the of The of of the and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, is in and is in the 1999; PubMed Scopus Google Scholar). expression was in of of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar, M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar). that from is fatty acid in the of and that of SCD and the in the of and its in the of is that of and its M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google Scholar). that the desaturase in the of is that of are four known Δ9-desaturase isoforms in mouse that are for the biosynthesis of monounsaturated fatty and J.M. Miyazaki M. Recent insights into stearoyl-CoA desaturase-1.Curr. Opin. Lipidol. 2003; 14: 255-261Crossref PubMed Scopus (207) Google Scholar). for The of Saccharomyces cerevisiae the delta 9 fatty acid desaturase and by the stearoyl-CoA desaturase Full Text PDF PubMed Google the substrate specificities of mammalian not been in the for the existence and expression of the multiple isoforms a that fatty acids for and of that mouse SCD isoforms substrate the from both and are of and there was SCD4 both and but the was of isoforms. the of SCD4 SCD3 uses C16:0 but not C18:0. this SCD3 A The substrate of protein Δ9-desaturase has been of the of the Shanklin J. J. A of substrate from the carrier protein desaturase of PubMed Scopus Google Scholar). and the at position was to the of Δ9-desaturase Shanklin J. J. A of substrate from the carrier protein desaturase of PubMed Scopus Google Scholar). of the in the the histidine and the are conserved in the mouse the distinct substrate the of mouse and are M. E. J.M. Ntambi J.M. and of a stearoyl-CoA desaturase isoform by and 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). The acid are in acid residues the histidine that acid in this of the protein as a of their are to this the for the existence of and its to monounsaturated fatty acids is it to the of the SCD and the in of their monounsaturated fatty acid is in lipid to as of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar). The monounsaturated fatty acid in is in fatty acid Full Text PDF PubMed Scopus Google Scholar). Because is is by the The of is that of to to and by and M. of of the Full Text Full Text PDF PubMed Scopus Google in the of The of of the and M. Ntambi J.M. of stearoyl-CoA in of and and of in the PubMed Scopus Google Scholar, is in and is in the 1999; PubMed Scopus Google Scholar). expression was in of of the stearoyl-CoA desaturase expression in PubMed Scopus Google Scholar, M. Ntambi J.M. of stearoyl-CoA a desaturase and the stearoyl-CoA in the of the Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar). that from is fatty acid in the of and that of SCD and the in the of and its in the of is that of and its M. Ntambi J.M. is the of stearoyl-CoA desaturase isoform and substrate for the biosynthesis of the Full Text Full Text PDF PubMed Scopus Google Scholar). that the desaturase in the of is that of was by of The for the