Information on EC 1.10.3.6 - rifamycin-B oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.10.3.6
-
RECOMMENDED NAME
GeneOntology No.
rifamycin-B oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
rifamycin B + O2 = rifamycin O + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative cyclization
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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).
CAS REGISTRY NUMBER
COMMENTARY hide
84932-52-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Humicola spp.
ATCC 20620
-
-
Manually annotated by BRENDA team
Monocillium spp.
ATCC 20621
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
catechol + O2
?
show the reaction diagram
Humicola spp.
-
-
-
-
?
p-hydroquinone + O2
?
show the reaction diagram
p-hydroxyphenoxyacetic acid + O2
?
show the reaction diagram
Humicola spp.
-
-
-
-
?
pyrogallol + ?
?
show the reaction diagram
Monocillium spp.
-
-
-
?
rifamycin B + O2
rifamycin O + H2O2
show the reaction diagram
rifamycin B + O2
rifamycin S + H2O2
show the reaction diagram
rifamycin SV + ?
?
show the reaction diagram
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
rifamycin B + O2
rifamycin O + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
Monocillium spp.
-
enzyme contains no flavins, heme, Cu2+ or other metal ions
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
60% inhibition at 20 mM
Co2+
-
slight inhibition
Cu2+
-
slight inhibition
NADH
Monocillium spp.
-
apparent inhibition
NADPH
Monocillium spp.
-
apparent inhibition
Rifamycin B
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
Monocillium spp.
-
slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.81
Rifamycin B
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.6
Rifamycin B
Humicola spp.
-
immobilized acetone-defatted cells
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.19
Monocillium spp.
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
Humicola spp.
-
-
7.8 - 8
Humicola spp.
-
-
7.8
Monocillium spp.
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
activity is studied in this range, above pH 7.0 the activity is reduced dramatically
5 - 10
Humicola spp.
-
-
6 - 7
-
80% of maximum activity at pH 6.0, activity declines sharply at a pH above 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
Monocillium spp.
-
assay at
40
Humicola spp.
-
assay at
45
Humicola spp.
-
above the catalytic activity is greatly reduced
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
-
activity is studied in this range
40 - 45
-
75-85% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
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+
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Humicola spp.
-
-
Manually annotated by BRENDA team
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
immobilized enzyme has a half life time of 11.5 days
60
-
soluble enzyme loses 80%, immobilized enzyme 50% of its maximum activity
additional information
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
increase by immobilization on polyacrylamide gel
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
helps improving activity
Ethanol
-
helps improving activity
Methanol
-
helps improving activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 100 mM phosphate buffer, pH 7.8, one month, no appreciable loss of actvity
Humicola spp.
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion-exchange, gel filtration
Monocillium spp.
-
partially, ammonium sulfate precipitation
Humicola spp.
-
partially, gel filtration
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine