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ENZYME entry: EC 1.14.19.23

Accepted Name
Acyl-lipid (n+3)-(Z)-desaturase (ferredoxin).
Alternative Name(s)
Acyl-lipid omega(6)-desaturase (ferredoxin).
Linoleate synthase.
Oleate desaturase.
Oleoyl-CoA desaturase.
Phosphatidylcholine desaturase.
Reaction catalysed
An oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O(2) + 2 H(+) <=> a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O
Comment(s)
  • This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids.
  • The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, toward the methyl end of the fatty acid.
  • The native substrates are oleoyl (18:1 Delta(9)) and (Z)-hexadec-7- enoyl (16:1 Delta(7)) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an omega(6) desaturase.
  • However, when acting on palmitoleoyl groups(16:1 Delta(9)), the enzyme introduces the second double bond at position 12 (omega(4)), indicating it is an (n+3) desaturase.
  • Cf. EC 1.14.19.34.
Cross-references
BRENDA1.14.19.23
EC2PDB1.14.19.23
ExplorEnz1.14.19.23
PRIAM enzyme-specific profiles1.14.19.23
KEGG Ligand Database for Enzyme Nomenclature1.14.19.23
IUBMB Enzyme Nomenclature1.14.19.23
IntEnz1.14.19.23
MEDLINEFind literature relating to 1.14.19.23
MetaCyc1.14.19.23
UniProtKB/Swiss-Prot
P46312, FAD6C_ARATH;  P48627, FAD6C_BRANA;  P48628, FAD6C_SOYBN;  
P48629, FAD6C_SPIOL;  

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