1.13.11.60: linoleate 8R-lipoxygenase
This is an abbreviated version!
For detailed information about linoleate 8R-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.60
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1.13.11.60
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hydroperoxide
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graminis
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gaeumannomyces
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oxylipins
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dioxygenation
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antarafacial
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8r-hydroperoxylinoleic
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allene
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aspergilli
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suprafacial
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cyclooxygenases
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ppoas
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verticillioides
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take-all
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homolytic
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zymoseptoria
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ferryl
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synthesis
- 1.13.11.60
- hydroperoxide
- graminis
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gaeumannomyces
- oxylipins
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dioxygenation
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antarafacial
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8r-hydroperoxylinoleic
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allene
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aspergilli
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suprafacial
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cyclooxygenases
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ppoas
- verticillioides
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take-all
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homolytic
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zymoseptoria
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ferryl
- synthesis
Reaction
Synonyms
5,8-LDS, 5,8-linoleate diol synthase, 6,8-diol synthase, 6R,8R-linoleate diol synthase, 6R,8RLDS, 7,8-diol synthase, 7,8-LDS, 7,8-linoleate diol synthase, 8(R)-dioxygenase, 8,11-hydroperoxide isomerase, 8-DOX, 8R-dioxygenase, 8R-DOX, 8R-DOX-5,8-LDS, 8R-DOX-7,8-LDS, 8R-DOX-LDS, dioxygenase-cytochrome P450, DOX-CYP, EC 1.13.11.44, EGE82165, FOXB_09952, GLRG_10013, linoleate 7,8-LDS, linoleate 8,11-LDS, linoleate diol synthase, linoleic acid 8R-dioxygenase, ODH51007, orphan DOX-CYP, PpoA
ECTree
1.13.11.60 linoleate 8R-lipoxygenaseAdvanced search results
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General Information on EC 1.13.11.60 - linoleate 8R-lipoxygenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively
metabolism
additional information
evolution
homologue dioxygenase-cytochrome P450 (DOX-CYP) is a fusion protein of the animal heme peroxidase (cyclooxygenase) superfamily. Phylogenetic tree of fungal fusion enzymes with homology to the animal heme peroxidase and CYP superfamilies, overview
evolution
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homologue dioxygenase-cytochrome P450 (DOX-CYP) is a fusion protein of the animal heme peroxidase (cyclooxygenase) superfamily. Phylogenetic tree of fungal fusion enzymes with homology to the animal heme peroxidase and CYP superfamilies, overview
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evolution
Colletotrichum graminicola M1.001 / M2 / FGSC 10212
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homologue dioxygenase-cytochrome P450 (DOX-CYP) is a fusion protein of the animal heme peroxidase (cyclooxygenase) superfamily. Phylogenetic tree of fungal fusion enzymes with homology to the animal heme peroxidase and CYP superfamilies, overview
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metabolism
fungal oxylipins can be formed by two subfamilies of cyclooxygenase-related DOX. The enzymatic activities of the DOX-CYP homologue of Colletotrichum graminicola and the DOX homologue of Fusarium oxysporum. The former oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid. The latter metabolizes fatty acids to hydroperoxides with broad substrate specificity. It oxidizes 20:4n-6 and 18:2n-6 to hydroperoxides with an R configuration at the (n-10) positions, and other n-6 fatty acids in the same way
metabolism
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fungal oxylipins can be formed by two subfamilies of cyclooxygenase-related DOX. The enzymatic activities of the DOX-CYP homologue of Colletotrichum graminicola and the DOX homologue of Fusarium oxysporum. The former oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid. The latter metabolizes fatty acids to hydroperoxides with broad substrate specificity. It oxidizes 20:4n-6 and 18:2n-6 to hydroperoxides with an R configuration at the (n-10) positions, and other n-6 fatty acids in the same way
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metabolism
Colletotrichum graminicola M1.001 / M2 / FGSC 10212
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fungal oxylipins can be formed by two subfamilies of cyclooxygenase-related DOX. The enzymatic activities of the DOX-CYP homologue of Colletotrichum graminicola and the DOX homologue of Fusarium oxysporum. The former oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid. The latter metabolizes fatty acids to hydroperoxides with broad substrate specificity. It oxidizes 20:4n-6 and 18:2n-6 to hydroperoxides with an R configuration at the (n-10) positions, and other n-6 fatty acids in the same way
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additional information
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Val-328 of 5,8-LDS does not influence the position of oxygenation in contrast to the homologous residues Val-349 of COX-1 and Leu-384 of 10R-dioxygenase. About 675 amino acids are sufficient to support 8-DOX activity
additional information
Val-328 of 5,8-LDS does not influence the position of oxygenation in contrast to the homologous residues Val-349 of COX-1 and Leu-384 of 10R-dioxygenase. About 675 amino acids are sufficient to support 8-DOX activity
