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1.14.19.3: acyl-CoA 6-desaturase

This is an abbreviated version!
For detailed information about acyl-CoA 6-desaturase, go to the full flat file.

Word Map on EC 1.14.19.3

Reaction

alpha-linolenoyl-CoA
+ 2 ferrocytochrome b5 +
O2
+ 2 H+ =
stearidonoyl-CoA
+ 2 ferricytochrome b5 + 2 H2O

Synonyms

acyl-CoA DELTA6-desaturase, acyl-CoA desaturase, acyl-CoA-dependent DELTA6-desaturase, AsD6DES, D6 desaturase, d6-des, D6D, D6Des, DEALTA6I, delta 6 desaturase, DELTA 6-desaturase, delta 6-fatty acid desaturase, DELTA-6 desaturase, delta-6 fatty acid desaturase, DELTA-6-desaturase, DELTA6 desaturase, DELTA6 fatty acid desaturase, DELTA6 fatty acyl desaturase, DELTA6-acyl CoA desaturase, DELTA6-acyl-group desaturase, DELTA6-desaturase, DELTA6-desaturase II, DELTA6-fatty acid desaturase, DELTA6-fatty acyl-CoA desaturase, delta61, DELTA6fad_b, DES6, desaturase, fatty acid DA6-, desaturase, linoleate, DesI, EaD6DES, EC 1.14.99.25, FA desaturase 2, FADS2, FADS6, fadsd6, FAT-3, fatty acid 6-desaturase, fatty acid DA6-desaturase, fatty acid DELTA 6-desaturase, fatty acid delta-6 desaturase, fatty acid DELTA6-desaturase, fatty acid desaturase 2, fatty acid desaturase-2, GcFADS2, linoleate desaturase, linoleic acid desaturase, linoleic desaturase, linoleoyl CoA desaturase, linoleoyl-coenzyme A desaturase, long-chain fatty acid DELTA6-desaturase, MaFADS6, MaFADS6-I, Md6, MpFADS6, PiDesD6, TpFADS2

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
                1.14.19.3 acyl-CoA 6-desaturase

Systematic Name

Systematic Name on EC 1.14.19.3 - acyl-CoA 6-desaturase

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SYSTEMATIC NAME
IUBMB Comments
linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
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.