Information on EC 1.13.11.76 - 2-amino-5-chlorophenol 1,6-dioxygenase

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The expected taxonomic range for this enzyme is: Comamonas testosteroni

EC NUMBER
COMMENTARY hide
1.13.11.76
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RECOMMENDED NAME
GeneOntology No.
2-amino-5-chlorophenol 1,6-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-chloronitrobenzene degradation
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SYSTEMATIC NAME
IUBMB Comments
2-amino-5-chlorophenol: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 from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.74, 2-aminophenol 1,6-dioxygenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit alpha
UniProt
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-5-chlorophenol + O2
2-amino-5-chloromuconate 6-semialdehyde
show the reaction diagram
68% of the activity with 2-aminophenol
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?
2-aminophenol + O2
?
show the reaction diagram
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?
catechol + O2
?
show the reaction diagram
5% of the activity with 2-aminophenol
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?
protocatechuate + O2
?
show the reaction diagram
33% of the activity with 2-aminophenol
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?
additional information
?
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no substrates: 4-methylcatechol, 4-chlorocatechol, 2,4-dihydroxybenzoic acid, o-nitrophenol, p-nitrophenol, and 4-nitrocatechol
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
2 mM, 79% residual activity
Cd2+
2 mM abolishes enzyme activity completely
Co2+
2 mM abolishes enzyme activity completely
Cu2+
2 mM, 2.9% residual activity
EDTA
2 mM, 50% residual activity
Fe2+
2 mM, 57% residual activity. Not inhibitory in presence of ascorbate
H2O2
2 mM, complete loss of activity
Mg2+
2 mM, 91% residual activity
Mn2+
2 mM, 31% residual activity
Ni2+
2 mM abolishes enzyme activity completely
Zn2+
2 mM abolishes enzyme activity completely
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00077
2-amino-5-chlorophenol
pH 8.0, 22°C
0.00089
2-Aminophenol
pH 8.0, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29.7
pH 8.0, 22°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
2 * 33000, alpha-subunit, + 2 * 38000, beta-subunit, SDS-PAGE
38000
2 * 33000, alpha-subunit, + 2 * 38000, beta-subunit, SDS-PAGE
130000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
2 * 33000, alpha-subunit, + 2 * 38000, beta-subunit, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli