The Enzyme Database

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Accepted name: rifampicin monooxygenase
Reaction: rifampicin + NAD(P)H + O2 = 2′-N-hydroxyrifampicin + NAD(P)+ + H2O
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
Systematic name: rifampicin:NAD(P)H:oxygen oxidoreductase (2′-N-hydroxyrifampicin-forming)
Comments: The enzyme has been found in the Corynebacteria Rhodococcus equi and Nocardia farcinica. It confers increased resistance to the antibiotic rifampicin by initiating its degradation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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]
[EC created 2016]
Accepted name: rifampicin phosphotransferase
Reaction: ATP + rifampicin + H2O = AMP + 21-phosphorifampicin + phosphate
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
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]
[EC created 2018]

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