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Information on EC 1.13.11.74 - 2-aminophenol 1,6-dioxygenase and Organism(s) Comamonas testosteroni and UniProt Accession Q6J1Z6

for references in articles please use BRENDA:EC1.13.11.74
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IUBMB 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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UNIPROT: Q6J1Z6 not found.
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The taxonomic range for the selected organisms is: Comamonas testosteroni
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2-aminophenol 1,6-dioxygenase, amnba, 2-aminophenol-1,6-dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amnA
-
-
-
-
amnB
-
-
-
-
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].
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-5-chlorophenol + O2
?
show the reaction diagram
68% activity compared to 2-aminophenol
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
show the reaction diagram
protocatechuate + O2
?
show the reaction diagram
33% activity compared to 2-aminophenol
-
-
?
additional information
?
-
5% activity with catechol
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
68% activity compared to 2-aminophenol
-
-
?
2-aminophenol + O2
2-aminomuconate 6-semialdehyde
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
the enzyme contains Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrocatechol
Ca2+
79.4% residual activity at 2 mM
catechol
-
the enzyme completely loses its activity towards 2-aminophenol after incubation with catechol for 100 s
Cd2+
abolishes enzyme activity completely at 2 mM
Co2+
abolishes enzyme activity completely at 2 mM
Cu2+
2.9% residual activity at 2 mM
Fe2+
57.4% residual activity at 2 mM
Fe3+
4.4% residual activity at 2 mM
H2O2
abolishes enzyme activity completely at 2 mM
K3Fe(CN)6
41.2% residual activity at 2 mM
Mg2+
91.2% residual activity at 2 mM
Mn2+
30.9% residual activity at 2 mM
Ni2+
abolishes enzyme activity completely at 2 mM
Zn2+
abolishes enzyme activity completely at 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00077
2-amino-5-chlorophenol
in 10 mM sodium phosphate buffer, at pH 8.0 and 22°C
0.00089 - 0.0171
2-Aminophenol
0.0775
O2
-
at pH 8.0, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
EDTA
Comamonas testosteroni
in 10 mM sodium phosphate buffer, at pH 8.0 and 22°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMNB_COMTE
312
0
35040
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
gel filtration
140000
gel filtration
29000
2 * 35000 + 2 * 29000, calculated from amino acid sequence
30000
2 * 35000 + 2 * 30000, SDS-PAGE
33000
2 * 38000 + 2 * 33000, SDS-PAGE
35000
38000
2 * 38000 + 2 * 33000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E251A
-
inactive
H13A
-
inactive
H195Q
-
inactive
H62A
-
inactive
Y129F
-
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Mono Q column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team