EC Number   |
General Information |
Reference  |
|---|
   1.13.11.60 | malfunction |
replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively |
711024 |
| 1.13.11.60 | more |
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 |
711024 |
| 1.13.11.60 | more |
homology model of 5,8-LDS, overview |
724132 |
| 1.13.11.60 | more |
homology model of 7,8-LDS, overview |
724132 |
| 1.13.11.60 | 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 |
-, 743200 |
| 1.13.11.60 | 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 |
-, 743200 |
