The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions.
| Predicate | Object |
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| rdf:type | |
| rdfs:comment |
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 Aspergillus nidulans uses different heme domains to catalyze two separate reactions.,
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).
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| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
5,8-linoleate diol synthase (bifunctional enzyme),
7,8-linoleate diol synthase (bifunctional enzyme),
Linoleate 8R-lipoxygenase
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| uniprot:replaces | |
| uniprot:activity |
Linoleate + O(2) = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate.
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| uniprot:cofactor |
Heme
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