KEGG   ENZYME: 1.14.19.6Help
Entry
EC 1.14.19.6                Enzyme                                 

Name
Delta12-fatty-acid desaturase;
Delta12 fatty acid desaturase;
Delta12(omega6)-desaturase;
oleoyl-CoA Delta12 desaturase;
Delta12 desaturase;
Delta12-desaturase
Class
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
BRITE hierarchy
Sysname
acyl-CoA,hydrogen donor:oxygen Delta12-oxidoreductase
Reaction(IUBMB)
acyl-CoA + reduced acceptor + O2 = Delta12-acyl-CoA + acceptor + 2 H2O
Substrate
acyl-CoA [CPD:C00040];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
Delta12-acyl-CoA;
acceptor [CPD:C00028];
H2O [CPD:C00001]
Comment
In the yeast Lipomyces starkeyi [3] and in the American cockroach [1], this microsomal enzyme converts oleoyl-CoA into linoleoyl-CoA. In the moths Cadra cautella and Spodoptera, the enzyme converts (Z)-tetradec-9-enoic acid into (9Z,12E)-tetradeca-9,12-dienoic acid, which is reduced and acetylated to form the acetate ester pheromone [2].
Reference
1  [PMID:2248971]
  Authors
Borgeson CE, de Renobales M, Blomquist GJ.
  Title
Characterization of the delta 12 desaturase in the American cockroach, Periplaneta americana: the nature of the substrate.
  Journal
Biochim. Biophys. Acta. 1047 (1990) 135-40.
  Organism
Periplaneta americana
Reference
2  [PMID:9230926]
  Authors
Jurenka RA.
  Title
Biosynthetic pathway for producing the sex pheromone component (Z,E)-9,12-tetradecadienyl acetate in moths involves a delta 12 desaturase.
  Journal
Cell. Mol. Life. Sci. 53 (1997) 501-5.
  Organism
Cadra cautella
Reference
3  [PMID:8900454]
  Authors
Lomascolo A, Dubreucq E, Galzy P.
  Title
Study of the delta 12-desaturase system of Lipomyces starkeyi.
  Journal
Lipids. 31 (1996) 253-9.
  Organism
Lipomyces starkeyi
Reference
4  [PMID:9829122]
  Authors
Tocher DR, Leaver MJ, Hodgson PA.
  Title
Recent advances in the biochemistry and molecular biology of fatty acyl desaturases.
  Journal
Prog. Lipid. Res. 37 (1998) 73-117.
  Organism
Synechocystis sp. [GN:syn], Synechococcus sp. [GN:syp]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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