KEGG   ENZYME: 2.3.1.147Help
Entry
EC 2.3.1.147                Enzyme                                 

Name
glycerophospholipid arachidonoyl-transferase (CoA-independent)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine arachidonoyltransferase (CoA-independent)
Reaction(IUBMB)
1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine [RN:R04720]
Reaction(KEGG)
Substrate
1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine;
1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine [CPD:C05209]
Product
1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine;
1-organyl-2-lyso-sn-glycero-3-phosphocholine [CPD:C04317]
Comment
Catalyses the transfer of arachidonate and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.148 glycerophospholipid acyltransferase (CoA-dependent) in not requiring CoA and in its specificity for poly-unsaturated acyl groups.
History
EC 2.3.1.147 created 1999
Reference
1  [PMID:4008481]
  Authors
Robinson M, Blank ML, Snyder F.
  Title
Acylation of lysophospholipids by rabbit alveolar macrophages. Specificities of CoA-dependent and CoA-independent reactions.
  Journal
J. Biol. Chem. 260 (1985) 7889-95.
Reference
2  [PMID:1641397]
  Authors
Snyder F, Lee TC, Blank ML.
  Title
The role of transacylases in the metabolism of arachidonate and platelet activating factor.
  Journal
Prog. Lipid. Res. 31 (1992) 65-86.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
102347-79-5

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