| EC |
2.7.9.6 |
| Accepted name: |
rifampicin phosphotransferase |
| Reaction: |
ATP + rifampicin + H2O = AMP + 21-phosphorifampicin + phosphate |
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For diagram of rifampicin, click here |
| Glossary: |
rifampicin = rifampin = 3-[(4-methylpiperazin-1-yl)iminomethyl]rifamycin |
| Other name(s): |
rifampin phosphotransferase; RPH |
| Systematic name: |
ATP:rifampicin, water 21-O-phosphotransferase |
| Comments: |
The enzyme, characterized from a diverse collection of Gram-positive bacteria, inactivates the antibiotic rifampicin by phosphorylating it at position 21. The enzyme comprises three domains: two substrate-binding domains (ATP-grasp and rifampicin-binding domains) and a smaller phosphate-carrying L-histidine swivel domain that transits between the spatially distinct substrate-binding sites during catalysis. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Spanogiannopoulos, P., Waglechner, N., Koteva, K. and Wright, G.D. A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria. Proc. Natl. Acad. Sci. USA 111 (2014) 7102–7107. [DOI] [PMID: 24778229] |
| 2. |
Stogios, P.J., Cox, G., Spanogiannopoulos, P., Pillon, M.C., Waglechner, N., Skarina, T., Koteva, K., Guarne, A., Savchenko, A. and Wright, G.D. Rifampin phosphotransferase is an unusual antibiotic resistance kinase. Nat. Commun. 7:11343 (2016). [DOI] [PMID: 27103605] |
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| [EC 2.7.9.6 created 2018] |
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