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EC 1.14.19.44 Details
show Brenda entryEC 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
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.14.1.2 created 1965, deleted 1972 1.14.1.4 created 1965, deleted 1972 1.14.1.5 created 1965, deleted 1972 1.14.1.7 created 1965, deleted 1972 1.14.1.8 created 1965, deleted 1972 1.14.1.9 created 1965, deleted 1972 1.14.1.10 created 1965, deleted 1972 1.14.1.11 created 1965, deleted 1972
