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EC Explorer

EC 1.14.19.44 Details
EC number
1.14.19.44
Accepted name
acyl-CoA (8-3)-desaturase
Reaction
(1) (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = arachidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O;;(2) (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Other name(s)
FADS1 (gene name), acyl-CoA 5-desaturase (methylene-interrupted)
Systematic name
Δ8-acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (5,6-cis-dehydrogenating)
Comment
The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8. The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyse the desaturation of dihomo-γ-linoleate [(8Z,11Z,14Z)-icosa-8,11,14-trienoate] and (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome. cf. EC 1.14.19.37, acyl-CoA 5-desaturase.
History
created 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