Home  |  Contact

ENZYME entry: EC 1.14.19.31

Accepted Name
Acyl-lipid (7-3)-desaturase.
Alternative Name(s)
Acyl-lipid 4-desaturase.
Reaction catalysed
  • A (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
  • A (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
Comment(s)
  • The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond.
  • The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate.
  • The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
Cross-references
BRENDA1.14.19.31
EC2PDB1.14.19.31
ExplorEnz1.14.19.31
PRIAM enzyme-specific profiles1.14.19.31
KEGG Ligand Database for Enzyme Nomenclature1.14.19.31
IUBMB Enzyme Nomenclature1.14.19.31
IntEnz1.14.19.31
MEDLINEFind literature relating to 1.14.19.31
MetaCyc1.14.19.31
Rhea expert-curated reactions1.14.19.31
UniProtKB/Swiss-Prot
I2CYZ4, D4FAD_CHLRE;  Q6VPV2, D4FAD_DIALT;  Q6WNG7, D4FAD_EUGGR;  
A0PJ29, D4FAD_REBSA;  Q8S3C0, D4FAD_THRSP;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.19.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-