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Enzyme Nomenclature
Information on EC 1.14.13.211 - rifampicin monooxygenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.211
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RECOMMENDED NAME
GeneOntology No.
rifampicin monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
rifampicin + NAD(P)H + O2 = 2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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the rox gene is capable of initiating rifampicin degradation with another metabolite formation at the first step and having a role as the secondary rifampicin resistance factor in Nocardia farcinica
physiological function
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
physiological function
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the rox gene is capable of initiating rifampicin degradation with another metabolite formation at the first step and having a role as the secondary rifampicin resistance factor in Nocardia farcinica
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physiological function
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the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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-
?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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-
-
?
additional information
?
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the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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-
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additional information
?
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the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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-
-
-
?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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-
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?
additional information
?
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P95598
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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additional information
?
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P95598
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme
FAD
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enzyme Rox is a probable FAD-dependent monooxygenase because it contains the FAD-binding domain (Pfam accession number PF01494)
FAD
NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
LITERATURE
additional information
additional information
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the rox gene deletion mutation DELTArox gives no significant influence to the rifampicin resistance of Nocardia farcinica. Transformation with plasmid pKNL027_N05 overexpressing the rox gene markedly raises the rifampicin resistance in the strain with the deletion mutation of the rpoB2 gene as the principal rifampicin resistance determinant. Rifampicin is degraded by the wild-type strain, whereas it remains intact when incubated with the DELTArox strain
additional information
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the rox gene deletion mutation DELTArox gives no significant influence to the rifampicin resistance of Nocardia farcinica. Transformation with plasmid pKNL027_N05 overexpressing the rox gene markedly raises the rifampicin resistance in the strain with the deletion mutation of the rpoB2 gene as the principal rifampicin resistance determinant. Rifampicin is degraded by the wild-type strain, whereas it remains intact when incubated with the DELTArox strain
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.211)
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