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EC 1.14.19.5 Details
show Brenda entryEC number
1.14.19.5
Accepted name
acyl-CoA 11-(Z)-desaturase
Reaction
an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Other name(s)
Δ11 desaturase,
fatty acid Δ11-desaturase,
TpDESN,
Cro-PG,
Δ11 fatty acid desaturase,
Z/E11-desaturase,
Δ11-palmitoyl-CoA desaturase,
acyl-CoA,hydrogen donor:oxygen Δ11-oxidoreductase,
Δ11-fatty-acid desaturase
Systematic name
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (11,12 cis-dehydrogenating)
Comment
The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs. In moths the enzyme participates in the biosynthesis of their sex pheromones. The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0) [4], that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0) [5], while that from the moth Spodoptera littoralis accepts both substrates [1]. The enzyme contains three histidine boxes that are conserved in all desaturases [2]. It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase.
History
created 2008 (EC 1.14.99.32 created 2000, incorporated 2015), modified 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
