| EC |
1.14.13.211 |
| Accepted name: |
rifampicin monooxygenase |
| Reaction: |
rifampicin + NAD(P)H + O2 = 2-hydroxy-2,27-secorifampicin + NAD(P)+ + H2O |
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For diagram of rifampicin, click here |
| Glossary: |
rifampicin = (2S,12Z,14E,16S,17S,18R,19R,20R,21S,22R,23S,24E)-5,6,9,17,19-pentahydroxy-23-methoxy-2,4,12,16,18,20,22-heptamethyl-8-{[(E)-(4-methylpiperazin-1-yl)imino]methyl}-1,11-dioxo-1,2-dihydro-2,7-(epoxypentadeca-1,11,13-trienoimino)nathpho[2,1-b]furan-21-yl acetate |
| Other name(s): |
RIF-O; ROX; RIFMO; rifampicin:NAD(P)H:oxygen oxidoreductase (2′-N-hydroxyrifampicin-forming) (incorrect) |
| Systematic name: |
rifampicin:NAD(P)H:oxygen oxidoreductase (2-hydroxy-2,27-secorifampicin-forming; ring-cleaving) |
| Comments: |
The enzyme has been found in a variety of environmental bacteria, notably Rhodococcus, Nocardia, and Streptomyces. It hydroxylates C-2 of rifampicin leading to its macro-ring cleaving. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Andersen, S.J., Quan, S., Gowan, B. and Dabbs, E.R. Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic. Antimicrob. Agents Chemother. 41 (1997) 218–221. [PMID: 8980786] |
| 2. |
Hoshino, Y., Fujii, S., Shinonaga, H., Arai, K., Saito, F., Fukai, T., Satoh, H., Miyazaki, Y. and Ishikawa, J. Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance. J. Antibiot. (Tokyo) 63 (2010) 23–28. [DOI] [PMID: 19942945] |
| 3. |
Koteva, K., Cox, G., Kelso, J.K., Surette, M.D., Zubyk, H.L., Ejim, L., Stogios, P., Savchenko, A., Sørensen, D. and Wright, G.D. Rox, a rifamycin resistance enzyme with an unprecedented mechanism of action. Cell Chem Biol 25 (2018) 403–412.e5. [DOI] [PMID: 29398560] |
| 4. |
Liu, L.K., Dai, Y., Abdelwahab, H., Sobrado, P. and Tanner, J.J. Structural evidence for rifampicin monooxygenase inactivating rifampicin by cleaving Its ansa-bridge. Biochemistry 57 (2018) 2065–2068. [DOI] [PMID: 29578336] |
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| [EC 1.14.13.211 created 2016, modified 2022] |
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| 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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