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Literature summary for 1.14.13.211 extracted from

  • Liu, L.K.; Abdelwahab, H.; Martin Del Campo, J.S.; Mehra-Chaudhary, R.; Sobrado, P.; Tanner, J.J.
    The structure of the antibiotic deactivating, N-hydroxylating rifampicin monooxygenase (2016), J. Biol. Chem., 291, 21553-21562.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Nocardia farcinica

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Nocardia farcinica

Organism

Organism UniProt Comment Textmining
Nocardia farcinica Q5YTV5
-
-
Nocardia farcinica IFM 10152 Q5YTV5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
rifampicin + NAD(P)H + O2
-
Nocardia farcinica 2'-N-hydroxyrifampicin + NAD(P)+ + H2O
-
?
rifampicin + NAD(P)H + O2
-
Nocardia farcinica IFM 10152 2'-N-hydroxyrifampicin + NAD(P)+ + H2O
-
?

Synonyms

Synonyms Comment Organism
rifampicin monooxygenase
-
Nocardia farcinica
RifMO
-
Nocardia farcinica
rox
-
Nocardia farcinica

Cofactor

Cofactor Comment Organism Structure
FAD NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme Nocardia farcinica
NADPH NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme Nocardia farcinica