Cloned (Comment) | Organism |
---|---|
expression in a Streptomyces venezuelae pikC mutant | Saccharopolyspora erythraea |
Crystallization (Comment) | Organism |
---|---|
molecular modeling of the active site. For substrate narbomycin, the hydrophobic residues Ala223, Leu224, Leu225, and Leu226 may form hydrophobic interactions with the methyl group at C-6 and C-8 including C-7 of the macrolide ring | Saccharopolyspora erythraea |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharopolyspora erythraea | P48635 | erythromycin C-12 hydroxylase is able to substitute for pikromycin hydroxylase which is responsible for the hydroxylation of 10-deoxymethymycin and narbomycin. Erythromycin C-12 hydroxylase accepts both 12- and 14-membered macrolides | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Saccharopolyspora erythraea | methymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Saccharopolyspora erythraea | neomethymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
additional information | erythromycin C-12 hydroxylase is able to substitute for pikromycin hydroxylase which is responsible for the hydroxylation of 10-deoxymethymycin and narbomycin. Erythromycin C-12 hydroxylase accepts both 12- and 14-membered macrolides | Saccharopolyspora erythraea | ? | - |
? | |
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Saccharopolyspora erythraea | pikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
erythromycin C-12 hydroxylase | - |
Saccharopolyspora erythraea |