EC number:1.14.11.43
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: | 1.14.11.43 |
|---|---|
| Description: | (S)-dichlorprop dioxygenase (2-oxoglutarate). |
| Alternative Name: |
Alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase. 2-oxoglutarate-dependent (S)-mecoprop dioxygenase. 2-oxoglutarate-dependent (S)-dichlorprop dioxygenase. (S)-phenoxypropionate/alpha-ketoglutarate-dioxygenase. (S)-mecoprop dioxygenase. |
3D structure
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.11.43 |
| BRENDA Enzyme Link: | BRENDA 1.14.11.43 |
| KEGG Enzyme Link: | KEGG1.14.11.43 |
| BioCyc Enzyme Link: | BioCyc 1.14.11.43 |
| ExPASy Enzyme Link: | ExPASy1.14.11.43 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.11.43 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.11.43 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.11.43 |
| IntEnz Enzyme Link: | IntEnz 1.14.11.43 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.11.43 |
EC number:1.14.11.43
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:37831 | (S)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 2-methyl-4-chlorophenol + CO2 + pyruvate + succinate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]=[C;H0;+0:7](-[OH;+0:8])-[C;H0;+0:9](=[*:10])-[*:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:13].[*:5]-[OH;+0:4].[*:10]=[C;H0;+0:9](-[*:11])-[OH;+0:12].[*:6]=[C;H0;+0:7]=[O;H0;+0:8] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of two enantioselective alpha-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH. | Müller TA, Fleischmann T, van der Meer JR, Kohler HP | 2006 Jul | 16820480 |
| Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/alpha-ketoglutarate dioxygenases. | Müller TA, Zavodszky MI, Feig M, Kuhn LA, Hausinger RP | 2006 Jun | 16731970 |
| The two enantiospecific dichlorprop/alpha-ketoglutarate-dioxygenases from Delftia acidovorans MC1--protein and sequence data of RdpA and SdpA. | Westendorf A, Benndorf D, Müller RH, Babel W | 2002 | 12501996 |
| RHEA:37827 | (S)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + CO2 + pyruvate + succinate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]=[C;H0;+0:7](-[OH;+0:8])-[C;H0;+0:9](=[*:10])-[*:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:13].[*:5]-[OH;+0:4].[*:10]=[C;H0;+0:9](-[*:11])-[OH;+0:12].[*:6]=[C;H0;+0:7]=[O;H0;+0:8] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of two enantioselective alpha-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH. | Müller TA, Fleischmann T, van der Meer JR, Kohler HP | 2006 Jul | 16820480 |
| Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/alpha-ketoglutarate dioxygenases. | Müller TA, Zavodszky MI, Feig M, Kuhn LA, Hausinger RP | 2006 Jun | 16731970 |
| The two enantiospecific dichlorprop/alpha-ketoglutarate-dioxygenases from Delftia acidovorans MC1--protein and sequence data of RdpA and SdpA. | Westendorf A, Benndorf D, Müller RH, Babel W | 2002 | 12501996 |