KEGG   ENZYME: 1.14.19.5
Entry
EC 1.14.19.5                Enzyme                                 
Name
acyl-CoA 11-(Z)-desaturase;
Delta11 desaturase;
fatty acid Delta11-desaturase;
TpDESN;
Cro-PG;
Delta11 fatty acid desaturase;
Z/E11-desaturase;
Delta11-palmitoyl-CoA desaturase;
acyl-CoA,hydrogen donor:oxygen Delta11-oxidoreductase;
Delta11-fatty-acid desaturase
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,ferrocytochrome b5:oxygen oxidoreductase (11,12 cis-dehydrogenating)
Reaction(IUBMB)
an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrate
acyl-CoA [CPD:C00040];
ferrocytochrome b5 [CPD:C00999];
O2 [CPD:C00007];
H+ [CPD:C00080]
Product
(11Z)-enoyl-CoA;
ferricytochrome b5 [CPD:C00996];
H2O [CPD:C00001]
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
EC 1.14.19.5 created 2008 (EC 1.14.99.32 created 2000, incorporated 2015), modified 2015
Orthology
K18247  Delta11-fatty-acid desaturase
Genes
TPS: THAPS_23391(DES11)
Reference
1  [PMID:2295634]
  Authors
Martinez T, Fabrias G, Camps F
  Title
Sex pheromone biosynthetic pathway in Spodoptera littoralis and its activation by a neurohormone.
  Journal
J Biol Chem 265:1381-7 (1990)
Reference
2
  Authors
Rodriguez, F., Hallahan, D.L., Pickett, J.A. and Camps, F.
  Title
Characterization of the Delta11-palmitoyl-CoA-desaturase from Spodoptera littoralis (Lepidoptera:Noctuidae).
  Journal
Insect Biochem Mol Biol 22:143-148 (1992)
Reference
3
  Authors
Navarro, I., Font, I., Fabrias, G. and Camps, F.
  Title
Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone.
  Journal
J Am Chem Soc 119:11335-11336 (1997)
Reference
4  [PMID:15063718]
  Authors
Tonon T, Harvey D, Qing R, Li Y, Larson TR, Graham IA
  Title
Identification of a fatty acid Delta11-desaturase from the microalga Thalassiosira pseudonana.
  Journal
FEBS Lett 563:28-34 (2004)
DOI:10.1016/S0014-5793(04)00241-8
  Sequence
[tps:THAPS_23391]
Reference
5  [PMID:15455060]
  Authors
Hao G, O'Connor M, Liu W, Roelofs WL
  Title
Characterization of Z/E11- and Z9-desaturases from the obliquebanded leafroller moth, Choristoneura rosaceana.
  Journal
J Insect Sci 2:26 (2002)
DOI:10.1093/jis/2.1.26
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.5
IUBMB Enzyme Nomenclature: 1.14.19.5
ExPASy - ENZYME nomenclature database: 1.14.19.5
BRENDA, the Enzyme Database: 1.14.19.5

  All links  
Gene (2)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
Protein sequence (13)   
   UniProt (8)   
   SWISS-PROT (4)   
   RefSeq(pep) (1)   
DNA sequence (11)   
   RefSeq(nuc) (1)   
   GenBank (5)   
   EMBL (5)   
Protein domain (3)   
   InterPro (3)   
All databases (29)   

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