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ENZYME

ENZYME entry: EC 1.13.11.60

Accepted Name
linoleate 8R-lipoxygenase
Alternative Name(s)
5,8-linoleate diol synthase (bifunctional enzyme)
7,8-linoleate diol synthase (bifunctional enzyme)
Reaction catalysed
(9Z,12Z)-octadecadienoate + O2 <=> (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Comment(s)
  • The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions.
  • Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5).
  • The bifunctional enzyme from Gaeumannomyces graminis also catalyzes the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca- 9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)- 5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6).
  • Formerly EC 1.13.11.44.
Cross-references
BRENDA1.13.11.60
EC2PDB1.13.11.60
ExplorEnz1.13.11.60
PRIAM enzyme-specific profiles1.13.11.60
KEGG Ligand Database for Enzyme Nomenclature1.13.11.60
IUBMB Enzyme Nomenclature1.13.11.60
IntEnz1.13.11.60
MEDLINEFind literature relating to 1.13.11.60
MetaCyc1.13.11.60
Rhea expert-curated reactions1.13.11.60
UniProtKB/Swiss-Prot
Q9UUS2, LIDS_GAEGRG4N4J5, LIDS_PYRO7B0Y6R2, PPOA_ASPFC
Q4WPX2, PPOA_ASPFUQ6RET3, PPOA_EMENDG5EB19, PPOA_EMENI

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