KEGG   ENZYME: 1.14.19.37
Entry
EC 1.14.19.37               Enzyme                                 
Name
acyl-CoA 5-desaturase;
acyl-CoA 5-desaturase (non-methylene-interrupted)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
Sysname
acyl-CoA,acceptor:oxygen oxidoreductase (5,6 cis-dehydrogenating)
Reaction(IUBMB)
(1) (11Z,14Z)-icosa-11,14-dienoyl-CoA + reduced acceptor + O2 = (5Z,11Z,14Z)-icosa-5,11,14-trienoyl-CoA + acceptor + 2 H2O [RN:R11057];
(2) (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-CoA + reduced acceptor + O2 = (5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoyl-CoA + acceptor + 2 H2O [RN:R11058]
Reaction(KEGG)
R11057 R11058
Substrate
(11Z,14Z)-icosa-11,14-dienoyl-CoA [CPD:C16180];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007];
(11Z,14Z,17Z)-icosa-11,14,17-trienoyl-CoA [CPD:C16179]
Product
(5Z,11Z,14Z)-icosa-5,11,14-trienoyl-CoA [CPD:C21082];
acceptor [CPD:C00028];
H2O [CPD:C00001];
(5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoyl-CoA [CPD:C21083]
Comment
The enzyme, characterized from the plant Anemone leveillei, introduces a cis double bond at carbon 5 of acyl-CoAs that do not contain a double bond at position 8. In vivo it forms non-methylene-interrupted polyunsaturated fatty acids such as sciadonate and juniperonate. When expressed in Arabidopsis thaliana the enzyme could also act on unsaturated substrates such as palmitoyl-CoA. cf. EC 1.14.19.44, acyl-CoA (8-3)-desaturase.
History
EC 1.14.19.37 created 2015
Reference
1  [PMID:17384161]
  Authors
Sayanova O, Haslam R, Venegas Caleron M, Napier JA
  Title
Cloning and characterization of unusual fatty acid desaturases from Anemone leveillei: identification of an acyl-coenzyme A C20 Delta5-desaturase responsible for the synthesis of sciadonic acid.
  Journal
Plant Physiol 144:455-67 (2007)
DOI:10.1104/pp.107.098202
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.37
IUBMB Enzyme Nomenclature: 1.14.19.37
ExPASy - ENZYME nomenclature database: 1.14.19.37
BRENDA, the Enzyme Database: 1.14.19.37

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Chemical substance (8)   
   KEGG COMPOUND (8)   
Chemical reaction (3)   
   KEGG REACTION (2)   
   KEGG RCLASS (1)   
Protein sequence (7)   
   UniProt (4)   
   SWISS-PROT (3)   
DNA sequence (4)   
   GenBank (2)   
   EMBL (2)   
Protein domain (4)   
   InterPro (4)   
All databases (26)   

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