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ENZYME entry: EC 188.8.131.52
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|5,8-linoleate diol synthase (bifunctional enzyme).|
|7,8-linoleate diol synthase (bifunctional enzyme).|
|Linoleate + O(2) <=> (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate|
- 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.
- 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 184.108.40.206).
- Formerly EC 220.127.116.11.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
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