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Information on EC 1.13.11.74 - 2-aminophenol 1,6-dioxygenase
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1.13.11.74 2-aminophenol 1,6-dioxygenaseIUBMB Comments
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 . 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 .
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Word Map
- 1.13.11.74
-
2-aminomuconic
- dioxygenases
- nitrobenzene
- 6-semialdehyde
-
fission
-
extradiol
- protocatechuate
-
catecholic
-
dioxygenation
-
pseudoalcaligenes
-
meta-cleavage
- alpha-subunits
- comamonas
-
suicide
- beta-subunits
-
nonhaem
-
wastewater
- homoprotocatechuate
- 4-oxalocrotonate
- mutase
-
2-his-1-carboxylate
- nitroreductase
- 4-nitrocatechol
-
alpha2beta2
-
facial
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2-aminophenol 1,6-dioxygenase, amnba, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amnA
amnB
amnBA
APD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-4,5-dimethylphenol + O2
?
-
1.3% activity compared to 2-aminophenol
-
?
2-amino-4,5-dimethylphenol + O2
?
-
1.3% activity compared to 2-aminophenol
-
?
2-amino-4-chlorophenol + O2
?
-
15% activity compared to 2-aminophenol
-
?
2-amino-4-chlorophenol + O2
?
-
15% activity compared to 2-aminophenol
-
?
2-amino-4-chlorophenol + O2
?
-
6.8% activity compared to 2-aminophenol
-
?
2-amino-4-chlorophenol + O2
?
-
6.8% activity compared to 2-aminophenol
-
?
2-amino-5-chlorophenol + O2
?
68% activity compared to 2-aminophenol
-
?
2-amino-5-chlorophenol + O2
?
68% activity compared to 2-aminophenol
-
?
2-amino-m-cresol + O2
?
-
1% activity compared to 2-aminophenol
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
100% activity
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
100% activity
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
O34137; O24680
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
-
100% activity
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
-
100% activity
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
O34137; O24680
-
-
?
6-amino-m-cresol + O2
?
-
25% activity compared to 2-aminophenol
-
?
catechol + O2
?
O34137; O24680
suicide substrate of 2-aminophenol 1,6-dioxygenase
-
?
catechol + O2
?
O34137; O24680
suicide substrate of 2-aminophenol 1,6-dioxygenase
-
?
protocatechuate + O2
?
33% activity compared to 2-aminophenol
-
?
protocatechuate + O2
?
33% activity compared to 2-aminophenol
-
?
additional information
?
-
5% activity with catechol
-
?
additional information
?
-
5% activity with catechol
-
?
additional information
?
-
-
3-methylcatechol, 4-methylcatechol, 3-chlorocatechol, 4-chlorocatechol, 1,2,3-trihydroxybenzene, 1,2,4-trihydroxybenzene, 4-aminoresorcinol, 2-amino-p-cresol, 2,3-dihydroxybenzoic acid, protocatechuate, 2-methoxyphenol, 4-amino-3-hydroxybenzoic acid, 3-amino-4-hydroxybenzoic acid, 3-hydroxyanthranilic acid, and 4-amino-m-cresol are no substrates
-
?
additional information
?
-
-
3-methylcatechol, 4-methylcatechol, 3-chlorocatechol, 4-chlorocatechol, 1,2,3-trihydroxybenzene, 1,2,4-trihydroxybenzene, 4-aminoresorcinol, 2-amino-p-cresol, 2,3-dihydroxybenzoic acid, protocatechuate, 2-methoxyphenol, 4-amino-3-hydroxybenzoic acid, 3-amino-4-hydroxybenzoic acid, 3-hydroxyanthranilic acid, and 4-amino-m-cresol are no substrates
-
?
additional information
?
-
-
no activity with phenol, o-, m-, or p-cresol, aniline, o-, m-, or p-aminobenzoic acid, o-, m-, or p-phenylenediamine, protocatechuic acid, 2,3-dihydroxybenzoic acid, 3-aminophenol, 4-aminophenol, 2-amino-4-isopropylphenol, 2-amino-tert-butylphenol, 3-aminophenazin-2-ol, 2-amino-4-nitrophenol, 2-amino-5-nitrophenol, 3-amino-4-hydroxybenzoic acid, or 4-amino-3-hydroxybenzoic acid, amidol and 3-hydroxyanthralinic acid
-
?
additional information
?
-
-
no activity with phenol, o-, m-, or p-cresol, aniline, o-, m-, or p-aminobenzoic acid, o-, m-, or p-phenylenediamine, protocatechuic acid, 2,3-dihydroxybenzoic acid, 3-aminophenol, 4-aminophenol, 2-amino-4-isopropylphenol, 2-amino-tert-butylphenol, 3-aminophenazin-2-ol, 2-amino-4-nitrophenol, 2-amino-5-nitrophenol, 3-amino-4-hydroxybenzoic acid, or 4-amino-3-hydroxybenzoic acid, amidol and 3-hydroxyanthralinic acid
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-5-chlorophenol + O2
?
68% activity compared to 2-aminophenol
-
-
?
2-amino-5-chlorophenol + O2
?
68% activity compared to 2-aminophenol
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
-
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
100% activity
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
-
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
100% activity
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-nitrocatechol
-
suicide inhibitor, the enzyme completely loses its activity towards 2-aminophenol after incubation with 4-nitrocatechol for 100 s
catechol
-
the enzyme completely loses its activity towards 2-aminophenol after incubation with catechol for 100 s
catechol
O34137; O24680
the activity of the enzyme is restored after removal of catechol and incubation with ascorbate and FeCl2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00077
2-amino-5-chlorophenol
in 10 mM sodium phosphate buffer, at pH 8.0 and 22°C
0.00089
2-Aminophenol
in 10 mM sodium phosphate buffer, at pH 8.0 and 22°C
0.0171
2-Aminophenol
-
at pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
1,2,4-Trihydroxybenzene
-
pH and temperature not specified in the publication
0.0067
3-chlorocatechol
-
pH and temperature not specified in the publication
0.0054
3-fluorocatechol
-
pH and temperature not specified in the publication
0.0068
3-methylcatechol
-
pH and temperature not specified in the publication
0.0091
4-aminoresorcinol
-
pH and temperature not specified in the publication
0.0104
4-Chlorocatechol
-
pH and temperature not specified in the publication
0.0095
4-methylcatechol
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit alpha and catalytic subunit beta
UniProt
brenda
subunit alpha and catalytic subunit beta
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0L6Z9L6_9CLOT
469
0
52543
TrEMBL
-
A0A1V5M3B7_9FIRM
462
0
51496
TrEMBL
-
A0A143Y2U4_9FIRM
462
0
51547
TrEMBL
-
A0A2K9EP23_9FIRM
456
0
50749
TrEMBL
-
A0A2T0AXS7_9CLOT
469
0
52793
TrEMBL
-
A0A151ALB5_9CLOT
469
0
52793
TrEMBL
-
A0A1V5TS99_9FIRM
461
0
50240
TrEMBL
-
A0A1V5U4V5_9FIRM
461
0
49807
TrEMBL
-
A0A1E7RTU0_BUTME
461
0
50000
TrEMBL
-
A0A094J1U9_9BACT
460
0
51725
TrEMBL
-
A0A1Q9NYX2_9ARCH
262
0
29591
TrEMBL
-
A0A1V5QE95_9CHLR
459
0
50826
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
29000
2 * 35000 + 2 * 29000, calculated from amino acid sequence
35000
35000
2 * 35000 + 2 * 29000, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterotetramer
heterotetramer
2 * 35000 + 2 * 29000, calculated from amino acid sequence
heterotetramer
-
2 * 35000 + 2 * 29000, calculated from amino acid sequence
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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
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
the enzyme loses 50% of its activity upon incubation at 60°C for 5 min
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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
-20°C, 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
-
ammonium sulfate precipitation, Mono Q column chromatography, and Superdex 200 gel filtration
ethanol precipitation, MonoQ column chromatography, and Sephacryl S-300 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takenaka, S.; Murakami, S.; Kim, Y.J.; Aoki, K.
Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3
Arch. Microbiol.
174
265-272
2000
Pseudomonas sp., Pseudomonas sp. Ap-3
brenda
Li, d.e..F.; Zhang, J.Y.; Hou, Y.J.; Liu, L.; Hu, Y.; Liu, S.J.; Wang, d.a..C.; Liu, W.
Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor
Acta Crystallogr. Sect. D
69
32-43
2013
Comamonas testosteroni, Comamonas testosteroni CNB-1
brenda
Li, D.F.; Zhang, J.Y.; Hou, Y.; Liu, L.; Liu, S.J.; Liu, W.
Crystallization and preliminary crystallographic analysis of 2-aminophenol 1,6-dioxygenase complexed with substrate and with an inhibitor
Acta Crystallogr. Sect. F
68
1337-1340
2012
Comamonas testosteroni (Q6J1Z5 and Q6J1Z6), Comamonas testosteroni CNB-1 (Q6J1Z5 and Q6J1Z6)
brenda
Davis, J.K.; He, Z.; Somerville, C.C.; Spain, J.C.
Genetic and biochemical comparison of 2-aminophenol 1,6-dioxygenase of Pseudomonas pseudoalcaligenes JS45 to meta-cleavage dioxygenases: divergent evolution of 2-aminophenol meta-cleavage pathway
Arch. Microbiol.
172
330-339
1999
Pseudomonas oleovorans (O34137 and O24680), Pseudomonas oleovorans JS45 (O34137 and O24680)
brenda
Wu, J.F.; Sun, C.W.; Jiang, C.Y.; Liu, Z.P.; Liu, S.J.
A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli
Arch. Microbiol.
183
1-8
2005
Comamonas testosteroni (Q6J1Z5 and Q6J1Z6), Comamonas testosteroni CNB-1 (Q6J1Z5 and Q6J1Z6)
brenda
Lendenmann, U.; Spain, J.C.
2-Aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45
J. Bacteriol.
178
6227-6232
1996
Pseudomonas oleovorans, Pseudomonas oleovorans JS45
brenda
Takenaka, S.; Murakami, S.; Shinke, R.; Hatakeyama, K.; Yukawa, H.; Aoki, K.
Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme
J. Biol. Chem.
272
14727-14732
1997
Pseudomonas sp., Pseudomonas sp. Ap-3
brenda
He, Z.; Spain, J.
Preparation of 2-aminomuconate from 2-aminophenol by coupled enzymatic dioxygenation and dehydrogenation reactions
J. Ind. Microbiol. Biotechnol.
23
138-142
1999
Pseudomonas oleovorans, Pseudomonas oleovorans JS45
brenda
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