EC number:1.14.11.20
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor |
| ID: | 1.14.11.20 | ||
|---|---|---|---|
| Description: | Deacetoxyvindoline 4-hydroxylase. | ||
| Alternative Name: |
Desacetyoxyvindoline-17-hydroxylase. Desacetoxyvindoline-4-hydroxylase. hydroxylating). Desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4-beta- D17H. | ||
| Prosite: | PDOC51471; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.11.20 |
| BRENDA Enzyme Link: | BRENDA 1.14.11.20 |
| KEGG Enzyme Link: | KEGG1.14.11.20 |
| BioCyc Enzyme Link: | BioCyc 1.14.11.20 |
| ExPASy Enzyme Link: | ExPASy1.14.11.20 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.11.20 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.11.20 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.11.20 |
| IntEnz Enzyme Link: | IntEnz 1.14.11.20 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.11.20 |
EC number:1.14.11.20
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:24865 | (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + 2-oxoglutarate + O2 = 4-O-deacetyl-16-O-demethylvindoline + CO2 + succinate |
| RULE(radius=1) | ([*:1]-[NH;+0:2]-[*:3]-[*:4]-[CH2;+0:5]-[*:6].[*:7]-[O;H0;+0:8]-[CH3;+0:9]).[*:10]=[C;H0;+0:11](-[OH;+0:12])-[C;H0;+0:13](=[*:14])-[*:15].[O;H0;+0:16]=[O;H0;+0:17]>>([*:1]-[N;H0;+0:2](-[CH3;+0:9])-[*:3]-[*:4]-[CH;+0:5](-[*:6])-[OH;+0:16].[*:7]-[OH;+0:8]).[*:14]=[C;H0;+0:13](-[*:15])-[OH;+0:17].[*:10]=[C;H0;+0:11]=[O;H0;+0:12] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in catharanthus roseus (L.) G. Don. . Evidence Of a multilevel regulatory mechanism | Vazquez-Flota FA, De Luca V | 1998 Aug | 9701591 |
| Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus. | De Carolis E, De Luca V | 1993 Mar 15 | 8449913 |
| Isolation and Characterization of a 2-Oxoglutarate Dependent Dioxygenase Involved in the Second-to-Last Step in Vindoline Biosynthesis. | De Carolis E, Chan F, Balsevich J, De Luca V | 1990 Nov | 16667836 |
| RHEA:18973 | 2-oxoglutarate + deacetoxyvindoline + O2 = 4-O-deacetylvindoline + CO2 + succinate |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in catharanthus roseus (L.) G. Don. . Evidence Of a multilevel regulatory mechanism | Vazquez-Flota FA, De Luca V | 1998 Aug | 9701591 |
| Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus. | De Carolis E, De Luca V | 1993 Mar 15 | 8449913 |
| Isolation and Characterization of a 2-Oxoglutarate Dependent Dioxygenase Involved in the Second-to-Last Step in Vindoline Biosynthesis. | De Carolis E, Chan F, Balsevich J, De Luca V | 1990 Nov | 16667836 |
| A pair of tabersonine 16-hydroxylases initiates the synthesis of vindoline in an organ-dependent manner in Catharanthus roseus. | Besseau S, Kellner F, Lanoue A, Thamm AM, Salim V, Schneider B, Geu-Flores F, Höfer R, Guirimand G, Guihur A, Oudin A, Glevarec G, Foureau E, Papon N, Clastre M, Giglioli-Guivarc'h N, St-Pierre B, Werck-Reichhart D, Burlat V, De Luca V, O'Connor SE, Courdavault V | 2013 Dec | 24108213 |