Information on EC 1.14.13.211 - rifampicin monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.211
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RECOMMENDED NAME
GeneOntology No.
rifampicin monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
rifampicin + NAD(P)H + O2 = 2'-N-hydroxyrifampicin + NAD(P)+ + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
rifampicin:NAD(P)H:oxygen oxidoreductase (2'-N-hydroxyrifampicin-forming)
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene iri
UniProt
Manually annotated by BRENDA team
gene iri
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
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assay at
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with rifampicin, to 1.8 A resolution. RifMO is a class A flavoprotein monooxygenase and is similar in fold and quaternary structure to MtmOIV and OxyS, in the mithramycin and oxytetracycline biosynthetic pathways, respectively. RifMO dimerizes via the FAD-binding domain to form a bell-shaped homodimer in solution with a maximal dimension of 110 A. The rifampicin naphthoquinone blocks access to the FAD N5 atom
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene iri, DNA and amino acid sequence determination and analysis, recombinant expression, the gene cloned from the Rhodococcus equi strain ATCC 14887 confers a 10fold increase in resistance to rifampin in Escherichia coli as well as a 25fold increase in Rhodococcus
gene rox, cloning and expression of wild-type and mutant enzymes in Escherichia coli strains JM109 and BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information