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EC 1.14.19.3 Details
EC number
1.14.19.3
Accepted name
acyl-CoA 6-desaturase
Reaction
(1) linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = γ-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O;;(2) α-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Other name(s)
Δ6-desaturase, Δ6-fatty acyl-CoA desaturase, Δ6-acyl CoA desaturase, fatty acid Δ6-desaturase, fatty acid 6-desaturase, linoleate desaturase, linoleic desaturase, linoleic acid desaturase, linoleoyl CoA desaturase, linoleoyl-coenzyme A desaturase, long-chain fatty acid Δ6-desaturase, linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase, linoleoyl-CoA desaturase, FADS2 (gene name)
Systematic name
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (6,7 cis-dehydrogenating)
CAS registry number
9082-66-0
Comment
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.
History
created 1986 as EC 1.14.99.25, transferred 2000 to EC 1.14.19.3, modified 2015
EC Tree
1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000
1.14.99.6 created 1972, modified 2000, deleted 2000
1.14.99.8 created 1972, deleted 1984
1.14.99.13 created 1972, deleted 1984
1.14.99.16 created 1972, deleted 2002
1.14.99.17 created 1972, deleted 1976
1.14.99.18 created 1976, modified 1999, deleted 2003
1.14.99.25 created 1986, deleted 2000