Information on EC 3.7.1.13 - 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.7.1.13
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = anthranilate + (2E)-2-hydroxypenta-2,4-dienoate
show the reaction diagram
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carbazole degradation
-
-
Dioxin degradation
-
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Metabolic pathways
-
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate acylhydrolase
This enzyme catalyses the third step in the aerobic degradation pathway of carbazole. The effect of the presence of an amino group or hydroxyl group at the 2-position of the substrate is small. The enzyme has no cofactor requirement [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain LD2
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-
Manually annotated by BRENDA team
strain LD2
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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-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid + H2O
benzoic acid + 2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
show the reaction diagram
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
?
show the reaction diagram
2-hydroxymuconic semialdehyde + H2O
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
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pH 7.5, 25C
0.00251 - 0.00273
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
Pseudomonas sp.
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pH 7.5, 25C
1.99 - 2.14
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
730 - 852
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
2066
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2600
-
pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
no activity
9
-
about 50% of maximal activity
10.5
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no activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
2 * 31000, SDS-PAGe, 2 * 31300, calculated
31300
2 * 31000, SDS-PAGe, 2 * 31300, calculated
32231
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x * 32231, calculated, x * 33000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.86 A resolution, space group I422. The subunit of ht-CarCJ3 is divided into two domains, i.e., the core domain with residues 15-144 and 209-282, and the lid domain with residues 145-208. The invisible 10 amino acid residues Ile146-Asn155 correspond to the helix alpha4, which is the putative first alpha-helix in the lid domain. Sidechains of the active-site residues, Ser114 and His261, are clearly shown in the electron density map
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
10 min, 75% residual activity
65
10 min, inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinantv enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE