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ENZYME entry: EC 1.14.19.5

Accepted Name
Acyl-CoA 11-(Z)-desaturase.
Alternative Name(s)
Delta(11) desaturase.
Delta(11)-fatty-acid desaturase.
Delta(11)-palmitoyl-CoA desaturase.
Fatty acid Delta(11)-desaturase.
Z/E11-desaturase.
Reaction catalysed
An acyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O
Comment(s)
  • 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), that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0), while that from the moth Spodoptera littoralis accepts both substrates.
  • The enzyme contains three histidine boxes that are conserved in all desaturases.
  • 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.
  • Formerly EC 1.14.19.n2 and EC 1.14.99.32.
Cross-references
BRENDA1.14.19.5
EC2PDB1.14.19.5
ExplorEnz1.14.19.5
PRIAM enzyme-specific profiles1.14.19.5
KEGG Ligand Database for Enzyme Nomenclature1.14.19.5
IUBMB Enzyme Nomenclature1.14.19.5
IntEnz1.14.19.5
MEDLINEFind literature relating to 1.14.19.5
MetaCyc1.14.19.5
UniProtKB/Swiss-Prot
Q8ISS3, ACO11_CHORO;  Q6US81, ACO11_SPOLI;  O44390, ACO11_TRINI;  
Q75PL7, DESAT_BOMMO;  

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