Information on EC 1.13.11.74 - 2-aminophenol 1,6-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.74
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RECOMMENDED NAME
GeneOntology No.
2-aminophenol 1,6-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-aminophenol degradation
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4-nitrotoluene degradation II
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Aminobenzoate degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
2-aminophenol:oxygen 1,6-oxidoreductase (decyclizing)
The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme also has some activity with 2-amino-5-methylphenol and 2-amino-4-methylphenol [1]. The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.76, 2-amino-5-chlorophenol 1,6-dioxygenase [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
2-amino-4,5-dimethylphenol + O2
?
show the reaction diagram
2-amino-4-chlorophenol + O2
?
show the reaction diagram
2-amino-5-chlorophenol + O2
?
show the reaction diagram
2-amino-m-cresol + O2
?
show the reaction diagram
2-amino-p-cresol + O2
?
show the reaction diagram
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
show the reaction diagram
6-amino-m-cresol + O2
?
show the reaction diagram
catechol + O2
?
show the reaction diagram
protocatechuate + O2
?
show the reaction diagram
additional information
?
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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-amino-5-chlorophenol + O2
?
show the reaction diagram
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3-Trihydroxybenzene
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complete inhibition at 0.05 mM
1,2,4-Trihydroxybenzene
2,2'-dipyridyl
2,3-Dihydroxybenzoic acid
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20% inhibition at 0.05 mM
2-amino-p-cresol
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90% inhibition at 0.05 mM
2-methoxyphenol
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30% inhibition at 0.05 mM
3-Amino-4-hydroxybenzoic acid
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20% inhibition at 0.05 mM
3-chlorocatechol
3-fluorocatechol
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noncompetitive inhibition
3-hydroxyanthranilic acid
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20% inhibition at 0.05 mM
3-methylcatechol
4-amino-3-hydroxybenzoic acid
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30% inhibition at 0.05 mM
4-amino-m-cresol
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10% inhibition at 0.05 mM
4-aminoresorcinol
4-Chlorocatechol
4-Methylcatechol
4-nitrocatechol
5,5'-dithiobis-(2-nitrobenzoic acid)
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complete inhibition at 0.5 mM
AgNO3
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6% residual activity at 0.5 mM
catechol
Cu2+
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2.9% residual activity at 2 mM
CuSO4
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complete inhibition at 0.1 mM
Fe2+
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57.4% residual activity at 2 mM
FeCl3
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complete inhibition at 0.5 mM
FeSO4(NH4)2SO4
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78% residual activity at 0.5 mM
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HgCl2
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12% residual activity at 0.5 mM
iodoacetate
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40% residual activity at 0.5 mM
K3Fe(CN)6
MgSO4
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79% residual activity at 0.5 mM
MnCl2
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53% residual activity at 0.5 mM
Mo2+
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96% residual activity at 2 mM
N-ethylmaleimide
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83% residual activity at 0.5 mM
NaN3
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complete inhibition at 0.5 mM
nitrilotriacetic acid
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86% residual activity at 2 mM
o-phenanthroline
p-chloromercuribenzoic acid
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65% residual activity at 0.5 mM
protocatechuate
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20% inhibition at 0.05 mM
pyrogallol
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noncompetitive inhibition
Tiron
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complete inhibition at 0.5 mM
additional information
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not inhibited by FeSO4
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00077
2-amino-5-chlorophenol
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in 10 mM sodium phosphate buffer, at pH 8.0 and 22C
0.00089 - 0.0467
2-Aminophenol
0.0775 - 0.71
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
147
2-Aminophenol
Pseudomonas pseudoalcaligenes
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in 50 mM Tris (pH 8.0) at 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.063
1,2,4-Trihydroxybenzene
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pH and temperature not specified in the publication
0.0067
3-chlorocatechol
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pH and temperature not specified in the publication
0.0054
3-fluorocatechol
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pH and temperature not specified in the publication
0.0068
3-methylcatechol
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pH and temperature not specified in the publication
0.0091
4-aminoresorcinol
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pH and temperature not specified in the publication
0.0104
4-Chlorocatechol
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pH and temperature not specified in the publication
0.0095
4-Methylcatechol
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pH and temperature not specified in the publication
0.0104
catechol
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pH and temperature not specified in the publication
0.0084
pyrogallol
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pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
EDTA
Comamonas testosteroni
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in 10 mM sodium phosphate buffer, at pH 8.0 and 22C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5
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crude extract, in 50 mM Tris (pH 8.0) at 25C
21.6
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purified enzyme, in 50 mM Tris (pH 8.0) at 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
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gel filtration
140000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
holoenzyme, with FeII and in complexes with the substrate 2-aminophenol and the suicide inhibitor 4-nitrocatechol, hanging drop vapor diffusion method, using 0.1 M sodium cacodylate pH 6.5, 25% (w/v) PEG 3350, 0.2 M sodium chloride
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in complex with (4Z,6Z)-3-iminooxepin-2(3H)-one, 2-aminomuconic 6-semialdehyde and 4-nitrocatechol, hanging drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.2 mM sodium chloride, 0.1 M sodium cacodylate pH 6.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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the enzyme loses 50% of its activity upon incubation at 60C for 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 50 mM MOPS (pH 7.3) containing ethanol (10% [v/v]) for 24 h abolishes 95% of the activity of 2-aminophenol 1,6-dioxygenase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified enzyme in 50 mM MOPS at pH 7.3 in the presence of 10% (v/v) glycerol, several months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetone precipitation, DE52-cellulose column chromatography, DEAE-cellulofine A-500 column chromatography, and gel filtration
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ammonium sulfate precipitation, Mono Q column chromatography, and Superdex 200 gel filtration
Q6J1Z5 and Q6J1Z6
ethanol precipitation, MonoQ column chromatography, and Sephacryl S-300 gel filtration
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partial purification
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
O34137 and O24680
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli JM109 cells
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expressed in Escherichia coli XL-1 Blue cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E251A
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inactive
H13A
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inactive
H195Q
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inactive
H62A
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inactive
Y129F
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inactive
E251A
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inactive
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H13A
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inactive
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H195Q
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inactive
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H62A
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inactive
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Y129F
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inactive
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