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EC Tree
IUBMB Comments Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC 1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC 1.10.3.5 (3-hydroxyanthranilate oxidase).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
rifamycin oxidase, rifamycin b oxidase,
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rifamycin B oxidase
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rifamycin B + O2 = rifamycin O + H2O2
rifamycin B + O2 = rifamycin O + H2O2
Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 catechol oxidase, EC 1.10.3.2 laccase, EC 1.10.3.4 o-aminophenol oxidase or EC 1.10.3.5 3-hydroxyanthranilate oxidase
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rifamycin B + O2 = rifamycin O + H2O2
acting on diphenols and related substances as electron donors and on oxygen as an electron acceptor
Monocillium spp.
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rifamycin B + O2 = rifamycin O + H2O2
acts on various kinds of diphenol compounds, converting them into quinonic forms and H2O2
Humicola spp.
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rifamycin B + O2 = rifamycin O + H2O2
immobilized enzyme
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rifamycin B + O2 = rifamycin O + H2O2
immobilized enzyme
Humicola spp.
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oxidative cyclization
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rifamycin-B:oxygen oxidoreductase
Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC 1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC 1.10.3.5 (3-hydroxyanthranilate oxidase).
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catechol + O2
?
Humicola spp.
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?
p-hydroxyphenoxyacetic acid + O2
?
Humicola spp.
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?
pyrogallol + ?
?
Monocillium spp.
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?
rifamycin B + O2
rifamycin O + H2O2
rifamycin B + O2
rifamycin S + H2O2
p-hydroquinone + O2
?
Humicola spp.
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?
p-hydroquinone + O2
?
Monocillium spp.
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rapid oxidation
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?
rifamycin B + O2
rifamycin O + H2O2
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-
?
rifamycin B + O2
rifamycin O + H2O2
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?
rifamycin B + O2
rifamycin O + H2O2
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?
rifamycin B + O2
rifamycin O + H2O2
Humicola spp.
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-
?
rifamycin B + O2
rifamycin O + H2O2
Humicola spp.
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-
?
rifamycin B + O2
rifamycin O + H2O2
Humicola spp.
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most specific, highest catalytic efficiency
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?
rifamycin B + O2
rifamycin O + H2O2
Monocillium spp.
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rapid oxidation
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?
rifamycin B + O2
rifamycin O + H2O2
Monocillium spp.
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reverse reaction of rifamycin B biosynthesis
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?
rifamycin B + O2
rifamycin S + H2O2
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?
rifamycin B + O2
rifamycin S + H2O2
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?
rifamycin SV + ?
?
Humicola spp.
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?
rifamycin SV + ?
?
Monocillium spp.
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?
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rifamycin B + O2
rifamycin O + H2O2
rifamycin B + O2
rifamycin O + H2O2
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?
rifamycin B + O2
rifamycin O + H2O2
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?
rifamycin B + O2
rifamycin O + H2O2
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?
rifamycin B + O2
rifamycin O + H2O2
Humicola spp.
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?
rifamycin B + O2
rifamycin O + H2O2
Humicola spp.
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?
rifamycin B + O2
rifamycin O + H2O2
Monocillium spp.
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reverse reaction of rifamycin B biosynthesis
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?
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additional information
Monocillium spp.
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enzyme contains no flavins, heme, Cu2+ or other metal ions
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additional information
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not affected by other metal ions than Fe2+, Hg2+, Ag+, Cu2+, Co2+ or EDTA
additional information
Humicola spp.
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not affected by other metal ions than Fe2+, Hg2+
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Ag+
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60% inhibition at 20 mM
NADH
Monocillium spp.
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apparent inhibition
NADPH
Monocillium spp.
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apparent inhibition
Fe2+
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90% inhibition at 20 mM
Hg2+
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complete inhibition at 20 mM
Rifamycin B
Humicola spp.
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concentration above 2 mM
Rifamycin B
Humicola spp.
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FAD
Monocillium spp.
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slight activation
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0.05
Rifamycin B
Humicola spp.
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0.3
Rifamycin B
Humicola spp.
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free acetone-defatted cells
0.6
Rifamycin B
Humicola spp.
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immobilized acetone-defatted cells
0.67 - 0.81
Rifamycin B
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19.6
Rifamycin B
Humicola spp.
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immobilized acetone-defatted cells
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3.19
Monocillium spp.
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7.8
Monocillium spp.
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assay at
7.8 - 8
Humicola spp.
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6.5
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6.5
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immobilized cells and soluble enzyme
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5 - 8
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activity is studied in this range, above pH 7.0 the activity is reduced dramatically
6 - 7
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80% of maximum activity at pH 6.0, activity declines sharply at a pH above 7.0
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37 - 40
Monocillium spp.
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assay at
40
Humicola spp.
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assay at
45
Humicola spp.
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above the catalytic activity is greatly reduced
50
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30 - 60
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activity is studied in this range
40 - 45
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75-85% of maximum activity
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brenda
Humicola spp.
ATCC 20620
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brenda
Monocillium spp.
ATCC 20621
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brenda
isolated from soil, hypomycetes
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brenda
MTCC 165
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var. aeri, isolated from soil
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brenda
var. aeria
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brenda
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additional information
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supplementation of malt extract shows pH close to neutral for 24 h followed by slight increase, whereas rifamycin oxidase productivity significantly enhanced (36 IU/ml) as compared to control (29 IU/ml) within 12 h. Rifamycin oxidase is considerably stimulated in presence of Ca2+, K+ and Na+. Chryseobacterium sp. shows increase in enzyme activity by 38.77% in presence of Ca2+ and K+ and 48.77% in presence of Na+
brenda
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brenda
Humicola spp.
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brenda
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50
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immobilized enzyme has a half life time of 11.5 days
60
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soluble enzyme loses 80%, immobilized enzyme 50% of its maximum activity
additional information
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immobilized enzyme has longer half life compared to free enzyme at 30°C and 40°C, the immobilized enzyme is more stable at higher temperatures
30
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immobilized enzyme has a half life time of 30 days
30
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half life of 9 days, after 7 days nearly 100% of activity is retained
40
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half life of 100 min, activity directly declined
40
Humicola spp.
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pH 8.0, half life time of 8 days
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increase by immobilization on polyacrylamide gel
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Acetone
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helps improving activity
Ethanol
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helps improving activity
Methanol
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helps improving activity
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4°C, 100 mM phosphate buffer, pH 7.8, one month, no appreciable loss of activity
Humicola spp.
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ammonium sulfate precipitation, ion-exchange, gel filtration
Monocillium spp.
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partially, ammonium sulfate precipitation
Humicola spp.
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partially, gel filtration
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medicine
Humicola spp.
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rifamycin is used for the treatment of tuberculosis
medicine
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starting material for synthesis of many clinically important rifampicins
medicine
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rifamycin S is used for the production of the antibiotic rifampicin for treatment of leprosy and tuberculosis
medicine
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rifamycin, an ansa-macrolide antibiotic, is used for production of antituberculosic agents
medicine
Humicola spp.
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rifamycin, an ansa-macrolide antibiotic, is used for production of antituberculosic agents
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Han, M.H.; Seong, B.L.; Son, H.J.; Mheen, T.I.
Rifamycin B oxidase from Monocillium spp., a new type of diphenol oxidase
FEBS Lett.
151
36-40
1983
Monocillium spp.
brenda
Vohra, R.M.; Banerjee, U.C.; Das, S.; Dube, S.
Microbial transformation of rifamycin B: a new extracellular oxidase from Curvularia lunata
Biotechnol. Lett.
11
851-854
1989
Curvularia lunata
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brenda
Seong, B.L.; Son, H.J.; Mheen, T.I.; Park, Y.H.; Han, M.H.
Enzymatic oxidation of rifamycins by a microorganism of the genus Humicola
J. Ferment. Technol.
63
515-522
1985
Humicola spp.
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brenda
Lee, G.M.; Choi, C.Y.
The properties of immobilized whole cell of Humicola spp. with rifamycin oxydase activity
Biotechnol. Lett.
6
143-148
1984
Humicola spp.
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brenda
Banerjee, U.C.
Transformation of rifamycin B with immobilized rifamycin oxidase of Curvularia lunata
Biotechnol. Tech.
7
339-344
1993
Curvularia lunata
brenda
Patil, B.B.; Chincholkar, S.B.
Influence of substrate preparation method on rifamycin oxidase activity of Curvularia lunata
Indian J. Exp. Biol.
35
917-919
1997
Curvularia lunata
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brenda
Banerjee, U.C.
Characterization of soluble rifamycin oxidase from Curvularia lunata var. aeria
Lett. Appl. Microbiol.
17
1-3
1993
Curvularia lunata
brenda
Jobanputra, A.H.; Chincholkar, S.B.
Influence of nitrogen sources and heavy metal ions on the production of rifamycin oxidase by Chryseobacterium sp.
J. Sci. Ind. Res.
66
615-617
2007
Chryseobacterium sp.
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brenda
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1.10.3.6 rifamycin-B oxidase
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