Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.13.211
Description:Rifampicin monooxygenase.
Alternative Name: RIF-O.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.13.211
BRENDA Enzyme Link: BRENDA 1.14.13.211
KEGG Enzyme Link: KEGG1.14.13.211
BioCyc Enzyme Link: BioCyc 1.14.13.211
ExPASy Enzyme Link: ExPASy1.14.13.211
EC2PDB Enzyme Link: EC2PDB 1.14.13.211
ExplorEnz Enzyme Link: ExplorEnz 1.14.13.211
PRIAM enzyme-specific profiles Link: PRIAM 1.14.13.211
IntEnz Enzyme Link: IntEnz 1.14.13.211
MEDLINE Enzyme Link: MEDLINE 1.14.13.211
MSA:

1.14.13.211;

Phylogenetic Tree:

1.14.13.211;

Uniprot:
M-CSA:
RHEA:48988 NADH + O2 + rifampicin = 2'-N-hydroxyrifampicin + H2O + NAD(+)
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[N;H0;+0:10]=[CH;+0:11]-[c;H0;+0:12]1:[c;H0;+0:13](-[OH;+0:14]):[*:15]:[*:16]:[c;H0;+0:17](-[*:18]):[c;H0;+0:19]:1-[*:20].[O;H0;+0:21]=[O;H0;+0:22]>>[*:9]-[N;H0;+0:10](-[OH;+0:21])-[CH;+0:11]=[C;H0;+0:12]1-[C;H0;+0:13](=[O;H0;+0:14])-[*:15]:[*:16]-[C;H0;+0:17](-[*:18])=[C;H0;+0:19]-1-[*:20].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:22]
Reaction
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References

TitleAuthorsDatePubMed ID
Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic.Andersen SJ, Quan S, Gowan B, Dabbs ER1997 Jan8980786
Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance.Hoshino Y, Fujii S, Shinonaga H, Arai K, Saito F, Fukai T, Satoh H, Miyazaki Y, Ishikawa J2010 Jan19942945

RHEA:46596 NADPH + O2 + rifampicin = 2'-N-hydroxyrifampicin + H2O + NADP(+)
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[N;H0;+0:10]=[CH;+0:11]-[c;H0;+0:12]1:[c;H0;+0:13](-[OH;+0:14]):[*:15]:[*:16]:[c;H0;+0:17](-[*:18]):[c;H0;+0:19]:1-[*:20].[O;H0;+0:21]=[O;H0;+0:22]>>[*:9]-[N;H0;+0:10](-[OH;+0:21])-[CH;+0:11]=[C;H0;+0:12]1-[C;H0;+0:13](=[O;H0;+0:14])-[*:15]:[*:16]-[C;H0;+0:17](-[*:18])=[C;H0;+0:19]-1-[*:20].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:22]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic.Andersen SJ, Quan S, Gowan B, Dabbs ER1997 Jan8980786
Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance.Hoshino Y, Fujii S, Shinonaga H, Arai K, Saito F, Fukai T, Satoh H, Miyazaki Y, Ishikawa J2010 Jan19942945