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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
1.4.99.1 D-amino-acid dehydrogenase
