Any feedback?
Literature summary for 1.14.13.154 extracted from
- The role of erythromycin C-12 hydroxylase, EryK, as a substitute for PikC hydroxylase in pikromycin biosynthesis (2004), Bioorg. Chem., 32, 549-559.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharopolyspora erythraea | P48635 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in a Saccharopolyspora venezuelae pikC deletion mutant, EryK can catalyze the hydroxylation of YC-17 and narbomycin to generate methymycin/neomethymycin and pikromycin, respectively. EryK is flexible toward some alternative polyketides and can be useful for structural diversification of macrolides by post-polyketide synthase hydroxylation | Saccharopolyspora erythraea | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EryK | - |
Saccharopolyspora erythraea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome P-450 | a heme-thiolate protein (P-450) | Saccharopolyspora erythraea |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
