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Information on EC 3.7.1.13 - 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase
for references in articles please use BRENDA:EC3.7.1.13
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EC Tree 3 Hydrolases
3.7 Acting on carbon-carbon bonds
3.7.1 In ketonic substances
3.7.1.13 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase
IUBMB Comments
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 .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, BphD, CarC, HOPDA hydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CarC
HOPDA hydrolase
CarC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = anthranilate + (2E)-2-hydroxypenta-2,4-dienoate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
carbazole degradation
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
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
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
2-hydroxypenta-2,4-dienoate + benzoate
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid + H2O
benzoic acid + 2-hydroxypenta-2,4-dienoic acid
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid + H2O
benzoic acid + 2-hydroxypenta-2,4-dienoic acid
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
?
Substrates: -
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?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
?
Substrates: -
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?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
Substrates: -
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Products: -
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
Substrates: -
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?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
Substrates: -
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?
2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
?
Substrates: 0.56% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Products: -
Products: -
?
2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
?
-
Substrates: 0.38% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Products: -
Products: -
?
2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
?
-
Substrates: 0.38% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Products: -
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?
2-hydroxymuconic semialdehyde + H2O
?
Substrates: 0.49% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Products: -
Products: -
?
2-hydroxymuconic semialdehyde + H2O
?
-
Substrates: 0.54% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Products: -
Products: -
?
2-hydroxymuconic semialdehyde + H2O
?
-
Substrates: 0.54% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: hydrolytic activity decreases in the substrate order of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate, 2-hydroxy-6-oxo-6-(2'-hydroxyphenyl)hexa-2,4-dienoate. Poor substrates: 2-hydroxy-6-oxohepta-2,4-dienoic acid, 2-hydroxymuconic semialdehyde
Products: -
Products: -
?
additional information
?
-
Substrates: hydrolytic activity decreases in the substrate order of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate, 2-hydroxy-6-oxo-6-(2'-hydroxyphenyl)hexa-2,4-dienoate. Poor substrates: 2-hydroxy-6-oxohepta-2,4-dienoic acid, 2-hydroxymuconic semialdehyde
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylmethylsulfonyl fluoride
-
about 10% residual activity at 1% (w/v)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0046
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
-
pH 7.5, 25°C
0.00251
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
pH 7.5, 25°C
0.00251
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
0.00273
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
more than 80% activity at 20-50°C, about 65% activity at 55°C, about 20% activity at 60°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). Q84II3_JANS3
Janthinobacterium sp. (strain J3)
290
0
32300
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D247A
-
the mutant shows 29.93% activity compared to the wild type enzyme
H275A
-
the mutant shows 10.25% activity compared to the wild type enzyme
S115A
-
the mutant shows 28.92% activity compared to the wild type enzyme
S114A
S114A
-
mutation in active-site serine. Approximately 40fold reduction in activity for the His-tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
S114A
-
mutation in active-site serine. Approximately 40fold reduction in activity for the His-tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Riddle, R.R.; Gibbs, P.R.; Willson, R.C.; Benedik, M.J.
Purification and properties of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase involved in microbial degradation of carbazole
Protein Expr. Purif.
28
182-189
2003
Pseudomonas sp., Pseudomonas sp. LD2
brenda
Habe, H.; Morii, K.; Fushinobu, S.; Nam, J.W.; Ayabe, Y.; Yoshida, T.; Wakagi, T.; Yamane, H.; Nojiri, H.; Omori, T.
Crystal structure of a histidine-tagged serine hydrolase involved in the carbazole degradation (CarC enzyme)
Biochem. Biophys. Res. Commun.
303
631-639
2003
Janthinobacterium sp. J3 (Q84II3), Metapseudomonas resinovorans, Metapseudomonas resinovorans CA10
brenda
Nojiri, H.; Taira, H.; Iwata, K.; Morii, K.; Nam, J.W.; Yoshida, T.; Habe, H.; Nakamura, S.; Shimizu, K.; Yamane, H.; Omori, T.
Purification and characterization of meta-cleavage compound hydrolase from a carbazole degrader Pseudomonas resinovorans strain CA10
Biosci. Biotechnol. Biochem.
67
36-45
2003
Metapseudomonas resinovorans (Q9AQM4), Metapseudomonas resinovorans CA10 (Q9AQM4)
brenda
Jia, Y.; Wang, J.; Ren, C.; Nahurira, R.; Khokhar, I.; Wang, J.; Fan, S.; Yan, Y.
Identification and characterization of a meta-cleavage product hydrolase involved in biphenyl degradation from Arthrobacter sp. YC-RL1
Appl. Microbiol. Biotechnol.
103
6825-6836
2019
Arthrobacter sp. YC-RL1
brenda
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