Information on EC 1.10.3.4 - o-aminophenol oxidase

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

EC NUMBER
COMMENTARY hide
1.10.3.4
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RECOMMENDED NAME
GeneOntology No.
o-aminophenol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
actinomycin D biosynthesis
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Tryptophan metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
2-aminophenol:oxygen oxidoreductase
A flavoprotein which catalyses a 6-electron oxidation. The enzyme from the plant Tecoma stans requires Mn2+ and FAD [1] whereas the fungus Pycnoporus coccineus requires Mn2+ and riboflavin 5'-phosphate [2], the bacteria Streptomyces antibioticus requires Cu2+ [4] and the plant Bauhenia monandra does not require any co-factors [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9013-85-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 2-aminophenol + 2 O2
isophenoxazine + 2 H2O + H2O2
show the reaction diagram
2-amino-4-methylphenol + O2
?
show the reaction diagram
3,4-dihydroxybenzaldehyde + O2
?
show the reaction diagram
3-amino-4-hydroxybenzaldehyde + O2
?
show the reaction diagram
3-hydroxyanthranilic acid + O2
2-amino-3-oxo-3H-phenoxazine-1,9-dicarboxylic acid + H2O
show the reaction diagram
3-hydroxykynurenine + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-3-hydroanthranilic acid methyl ester + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-3-hydroxyanthranilic acid + O2
?
show the reaction diagram
-
-
-
-
?
catechol + O2
?
show the reaction diagram
ferrocyanide + O2
?
show the reaction diagram
-
-
-
-
?
L-DOPA + O2
?
show the reaction diagram
o-aminophenol + O2
2-aminophenoxazin-3-one + H2O
show the reaction diagram
-
-
-
-
?
protocatchuic acid + O2
?
show the reaction diagram
-
-
-
-
?
protocatechuic acid + O2
?
show the reaction diagram
thiophenol + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
2 2-aminophenol + 2 O2
isophenoxazine + 2 H2O + H2O2
show the reaction diagram
2-amino-4-methylphenol + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxybenzaldehyde + O2
?
show the reaction diagram
-
-
-
-
?
3-amino-4-hydroxybenzaldehyde + O2
?
show the reaction diagram
-
-
-
-
?
3-hydroxyanthranilic acid + O2
2-amino-3-oxo-3H-phenoxazine-1,9-dicarboxylic acid + H2O
show the reaction diagram
3-hydroxykynurenine + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-3-hydroanthranilic acid methyl ester + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-3-hydroxyanthranilic acid + O2
?
show the reaction diagram
-
-
-
-
?
catechol + O2
?
show the reaction diagram
ferrocyanide + O2
?
show the reaction diagram
-
-
-
-
?
L-DOPA + O2
?
show the reaction diagram
protocatchuic acid + O2
?
show the reaction diagram
-
-
-
-
?
thiophenol + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
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involved in biosynthesis of catechol
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
riboflavin 5'-monophosphate
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holoenzyme reconstituted by addition of riboflavin 5'-phosphate and Mn2+
riboflavin 5'-phosphate
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-
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Dimercaptopropanol
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-
2-Aminophenol
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inhibitory above 0.6 mM
3-amino-4-hydroxybenzensulfonic acid
3-hydroxyanthranilic acid
4-hydroxy-3-nitrobenzaldehyde
4-hydroxybenzaldehyde
-
-
8-hydroxyquinoline
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-
alpha,alpha'-dipyridyl
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-
aniline
anthranilic acid
ascorbic acid
Atebrin
azide
cyanide
cysteine
glutathione
L-tyrosine
N-ethylmaleimide
o-aminophenol
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substrate inhibition above 0.6 mM
o-Nitrophenol
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p-chloromercuribenzoate
p-Hydroxybenzaldehyde
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p-hydroxymercuribenzoate
phenol
Sodium diethyldithiocarbamate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75
2-amino-4-methylphenol
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in 50 mM sodium phosphate, pH 7.0, 30°C
0.41
3,4-Dihydroxybenzaldehyde
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in 50 mM sodium phosphate, pH 7.0, 30°C
0.58
3-amino-4-hydroxybenzaldehyde
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in 50 mM sodium phosphate, pH 7.0, 30°C
19
catechol
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in 50 mM sodium phosphate, pH 7.0, 30°C
5.5
L-Dopa
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in 50 mM sodium phosphate, pH 7.0, 30°C
0.75 - 3.5
o-aminophenol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18
2-amino-4-methylphenol
Streptomyces griseus
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in 50 mM sodium phosphate, pH 7.0, 30°C
0.8
3,4-Dihydroxybenzaldehyde
Streptomyces griseus
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in 50 mM sodium phosphate, pH 7.0, 30°C
14
3-amino-4-hydroxybenzaldehyde
Streptomyces griseus
-
in 50 mM sodium phosphate, pH 7.0, 30°C
12
catechol
Streptomyces griseus
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in 50 mM sodium phosphate, pH 7.0, 30°C
0.066
L-Dopa
Streptomyces griseus
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in 50 mM sodium phosphate, pH 7.0, 30°C
20
o-aminophenol
Streptomyces griseus
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in 50 mM sodium phosphate, pH 7.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31
3-amino-4-hydroxybenzensulfonic acid
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-
3.9
4-hydroxy-3-nitrobenzaldehyde
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14
aniline
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3.2
L-tyrosine
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6.1
o-Nitrophenol
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1.9
p-Hydroxybenzaldehyde
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000035
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crude cell extract, at 30°C
0.066
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after 19000fold purification, at 30°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 7.6
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pH 4.6: about 50% of maximum activity, pH 7.6: about 65% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
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Superdex 200 gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
the enzyme remains active below 55°C at pH 7.0 for 20 min at various temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to extensive dialysis against cyanide or EDTA
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cu2+-charged HiTrap chelating HP column chromatography, HiTrap Q column chromatography and Resource PHE column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)/pLysS cells
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expression in Escherichia coli strain BL21(DE3). Optimization of phenoxazinone synthase production by response surface methodology via Box-Behnken design, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression is subject to glucose repression
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