Linoleate 8R-lipoxygenase

The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions.

Source:http://purl.uniprot.org/enzyme/1.13.11.60

Statements in which the resource exists.
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http://purl.uniprot.org/enz...rdfs:commentThe bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions.lld:uniprot
http://purl.uniprot.org/enz...rdfs:commentLinoleic 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).lld:uniprot
http://purl.uniprot.org/enz...rdfs:commentThe 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).lld:uniprot
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http://purl.uniprot.org/enz...uniprot:nameLinoleate 8R-lipoxygenaselld:uniprot
http://purl.uniprot.org/enz...uniprot:name5,8-linoleate diol synthase (bifunctional enzyme)lld:uniprot
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http://purl.uniprot.org/enz...uniprot:activityLinoleate + O(2) = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate.lld:uniprot
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