An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA , and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate . The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA [4], and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate [3]. The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
the FADS2 product introduces a double bond at the DELTA6, DELTA4 and DELTA8 positions by acting on at least ten substrates, including fatty acids 16:0, 18:2n-6, and 18:3n-3. MCF7 cells stably transformed with FADS2 biosynthesizes fatty acid 16:1n-10 from exogenous fatty acid 16:0, fatty acid 18:4n-3 from fatty acid 18:3n-3, fatty acid 18:3n-6 from fatty acid 18:2n-6, fatty acid 18:2n-9 from fatty acid 18:1n-9, fatty acid 24:6n-3 from fatty acid 24:5n-3 and fatty acid 24:5n-6 from fatty acid 24:4n-6