Information on EC 1.10.3.4 - o-aminophenol oxidase

for references in articles please use BRENDA:EC1.10.3.4
Word Map on EC 1.10.3.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

EC NUMBER
COMMENTARY hide
1.10.3.4
-
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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
actinomycin D biosynthesis
-
-
Tryptophan metabolism
-
-
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
-
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, 2'-azino-bis(3-ethyl benzothiazoline-6-sulfonic acid) + O2
?
show the reaction diagram
-
-
-
?
2-amino-4-methylphenol + O2
?
show the reaction diagram
2-aminophenol + O2
2-aminophenoxazin-3-one + H2O
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
-
-
-
-
?
2-aminophenol + O2
2-aminophenoxazin-3-one + H2O
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
?
-
-
involved in biosynthesis of catechol
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
riboflavin 5'-monophosphate
-
holoenzyme reconstituted by addition of riboflavin 5'-phosphate and Mn2+
riboflavin 5'-phosphate
-
-
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Dimercaptopropanol
-
-
2-Aminophenol
-
inhibitory above 0.6 mM
3-amino-4-hydroxybenzensulfonic acid
3-hydroxyanthranilic acid
4-hydroxy-3-nitrobenzaldehyde
4-hydroxybenzaldehyde
-
-
8-hydroxyquinoline
-
-
alpha,alpha'-dipyridyl
-
-
aniline
anthranilic acid
ascorbic acid
Atebrin
azide
cyanide
cysteine
DMSO
-
the native enzyme shows less than 5% residual activity in the presence of DMSO
ethanol
-
the native enzyme shows less than 5% residual activity in the presence of ethanol
ethyl acetate
-
the native enzyme shows less than 5% residual activity in the presence of ethyl acetate
glutathione
L-tyrosine
methanol
-
the native enzyme shows less than 5% residual activity in the presence of methanol
N-ethylmaleimide
o-aminophenol
-
substrate inhibition above 0.6 mM
o-Nitrophenol
-
-
p-chloromercuribenzoate
p-Hydroxybenzaldehyde
-
-
p-hydroxymercuribenzoate
phenol
Sodium diethyldithiocarbamate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75
2-amino-4-methylphenol
-
in 50 mM sodium phosphate, pH 7.0, 30C
0.052 - 0.077
2-Aminophenol
0.41
3,4-Dihydroxybenzaldehyde
-
in 50 mM sodium phosphate, pH 7.0, 30C
0.58
3-amino-4-hydroxybenzaldehyde
-
in 50 mM sodium phosphate, pH 7.0, 30C
19
catechol
-
in 50 mM sodium phosphate, pH 7.0, 30C
0.264
FMN
-
-
5.5
L-Dopa
-
in 50 mM sodium phosphate, pH 7.0, 30C
0.75 - 3.5
o-aminophenol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18
2-amino-4-methylphenol
-
in 50 mM sodium phosphate, pH 7.0, 30C
0.8
3,4-Dihydroxybenzaldehyde
-
in 50 mM sodium phosphate, pH 7.0, 30C
14
3-amino-4-hydroxybenzaldehyde
-
in 50 mM sodium phosphate, pH 7.0, 30C
12
catechol
-
in 50 mM sodium phosphate, pH 7.0, 30C
0.066
L-Dopa
-
in 50 mM sodium phosphate, pH 7.0, 30C
20
o-aminophenol
-
in 50 mM sodium phosphate, pH 7.0, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31
3-amino-4-hydroxybenzensulfonic acid
-
-
3.9
4-hydroxy-3-nitrobenzaldehyde
-
-
14
aniline
-
-
3.2
L-tyrosine
-
-
6.1
o-Nitrophenol
-
-
1.9
p-Hydroxybenzaldehyde
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000035
-
crude cell extract, at 30C
0.066
-
after 19000fold purification, at 30C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.5
-
enzyme on nanogel
4.5
-
free enzyme
8.5 - 10.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 7.6
-
pH 4.6: about 50% of maximum activity, pH 7.6: about 65% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
enzyme on nanogel
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
Superdex 200 gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
the enzyme remains active below 55C at pH 7.0 for 20 min at various temperatures
60
-
the native enzyme loses about 90% of its activity whereas the enzyme on nanogel loses about 50% of its activity after 2 h preincubation at 60C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to extensive dialysis against cyanide or EDTA
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 1 month
-
4C, enzyme on nanogel, 5 weeks, no loss of activity
-
4C, lyophilized enzyme, 5 weeks, 65% loss of activity
-
4C, native enzyme at pH 4.5, 5 weeks, 98% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cu2+-charged HiTrap chelating HP column chromatography, HiTrap Q column chromatography and Resource PHE column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)/pLysS cells
-
expression in Escherichia coli strain BL21(DE3). Optimization of phenoxazinone synthase production by response surface methodology via Box-Behnken design, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression is subject to glucose repression
-