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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 |
BRENDA | 1.13.11.60 |
EC2PDB | 1.13.11.60 |
ExplorEnz | 1.13.11.60 |
PRIAM enzyme-specific profiles | 1.13.11.60 |
KEGG Ligand Database for Enzyme Nomenclature | 1.13.11.60 |
IUBMB Enzyme Nomenclature | 1.13.11.60 |
IntEnz | 1.13.11.60 |
MEDLINE | Find literature relating to 1.13.11.60 |
MetaCyc | 1.13.11.60 |
Rhea expert-curated reactions | 1.13.11.60 |
UniProtKB/Swiss-Prot |
|
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