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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The enzyme appears in viruses and cellular organisms
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.
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
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
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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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
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
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
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
Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance
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1.14.13.211 rifampicin monooxygenase
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