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

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EC NUMBER
COMMENTARY hide
3.7.1.13
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RECOMMENDED NAME
GeneOntology No.
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase
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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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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carbazole degradation
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-
Dioxin degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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-
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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].
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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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
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
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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, 25°C
0.00251 - 0.00273
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
-
pH 7.5, 25°C
1.99 - 2.14
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
730 - 852
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2600
-
pH 7.5, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
no activity
9
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about 50% of maximal activity
10.5
-
no activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
Q84II3
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
10 min, 75% residual activity
65
10 min, inactivation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinantv enzyme
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 3.7.1.13)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)