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Information on EC 3.7.1.13 - 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase and Organism(s) Pseudomonas resinovorans and UniProt Accession Q9AQM4

for references in articles please use BRENDA:EC3.7.1.13
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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 .
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This record set is specific for:
Pseudomonas resinovorans
UNIPROT: Q9AQM4
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The taxonomic range for the selected organisms is: Pseudomonas resinovorans
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
CarC, HOPDA hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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].
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-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-oxo-6-phenylhexa-2,4-dienoate + H2O
?
show the reaction diagram
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
?
show the reaction diagram
-
0.38% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
2-hydroxymuconic semialdehyde + H2O
?
show the reaction diagram
-
0.54% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
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
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
2.14
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
852
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
CARC_PSERE
290
0
32252
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
2 * 31000, SDS-PAGe, 2 * 31300, calculated
31300
2 * 31000, SDS-PAGe, 2 * 31300, calculated
70000
gel filtration
33000
-
2 * 33000, SDS-PAGE
70000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 31000, SDS-PAGe, 2 * 31300, calculated
dimer
-
2 * 33000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
10 min, 75% residual activity
65
10 min, inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinantv enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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), Pseudomonas resinovorans, Pseudomonas resinovorans CA10
Manually annotated by BRENDA team
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
Pseudomonas resinovorans (Q9AQM4), Pseudomonas resinovorans CA10 (Q9AQM4)
Manually annotated by BRENDA team