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Literature summary extracted from
- Structural evidence for rifampicin monooxygenase inactivating rifampicin by cleaving its ansa-bridge (2018), Biochemistry, 57, 2065-2068 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.13.211 | structure of RIFMO in complex with the hydroxylated rifampicin product, to 2.10 A resolution. Structure shows a breach of the ansa aliphatic chain of rifampicin between naphthoquinone C2 and amide N1 | Nocardia farcinica |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.211 | Nocardia farcinica | Q5YTV5 | - |
- |
| 1.14.13.211 | Nocardia farcinica IFM 10152 | Q5YTV5 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.211 | RifMO | - |
Nocardia farcinica |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.13.211 | metabolism | RIFMO catalyzes the hydroxylation of rifampicin at the C2 atom followed by cleavage of the ansa linkage, which leads to inactivation of the antibiotic by preventing key contacts with the RNA polymerase target | Nocardia farcinica |
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Release 2023.1 (January 2023)
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