EC number:1.14.13.154
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.13.154 |
|---|---|
| Description: | Erythromycin 12 hydroxylase. |
| Cath: | 1.10.630.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.13.154 |
| BRENDA Enzyme Link: | BRENDA 1.14.13.154 |
| KEGG Enzyme Link: | KEGG1.14.13.154 |
| BioCyc Enzyme Link: | BioCyc 1.14.13.154 |
| ExPASy Enzyme Link: | ExPASy1.14.13.154 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.13.154 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.13.154 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.13.154 |
| IntEnz Enzyme Link: | IntEnz 1.14.13.154 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.13.154 |
EC number:1.14.13.154
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:32631 | erythromycin D + H(+) + NADPH + O2 = erythromycin C + H2O + NADP(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[CH;+0:10](-[*:11])-[*:12].[H+;H0:13].[O;H0;+0:14]=[O;H0;+0:15]>>[*:9]-[C;H0;+0:10](-[*:11])(-[*:12])-[OH;+0:14].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK. | Lambalot RH, Cane DE, Aparicio JJ, Katz L | 1995 Feb 14 | 7849045 |
| Azole drugs trap cytochrome P450 EryK in alternative conformational states. | Montemiglio LC, Gianni S, Vallone B, Savino C | 2010 Nov 2 | 20845962 |
| Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate. | Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B | 2009 Oct 16 | 19625248 |