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Information on EC - acyl-CoA 6-desaturase

for references in articles please use BRENDA:EC1.14.19.3
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IUBMB Comments
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.
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The enzyme appears in viruses and cellular organisms
fads2, delta-6 desaturase, delta6-desaturase, delta 6-desaturase, delta 6 desaturase, delta-6-desaturase, delta6 desaturase, fatty acid desaturase 2, delta6-fatty acid desaturase, fat-3, more
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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