EC - 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase

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IntEnz Enzyme Nomenclature


Accepted name:
9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
Other names:
5,8-LDS (bifunctional enzyme)
5,8-linoleate diol synthase (bifunctional enzyme)
8-hydroperoxide isomerase
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming)
Systematic name:
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate hydroxymutase [(5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate-forming]




The enzyme contains heme [3]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P450 heme thiolate domain [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Hoffmann, I., Jerneren, F., Garscha, U., Oliw, E. H.
    Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase.
    Arch. Biochem. Biophys. 506: 216-222 (2011). [PMID: 21130068]
  2. Jerneren, F., Garscha, U., Hoffmann, I., Hamberg, M., Oliw, E. H.
    Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus.
    Biochim. Biophys. Acta 1801: 503-507 (2010). [PMID: 20045744]
  3. Brodhun, F., Gobel, C., Hornung, E., Feussner, I.
    Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450.
    J. Biol. Chem. 284: 11792-11805 (2009). [PMID: 19286665]

[EC created 2011]