Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

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
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q84II3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
CarC, HOPDA hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CarC
-
-
-
-
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-phenylhexa-2,4-dienoate + H2O
?
show the reaction diagram
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
?
show the reaction diagram
0.56% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
2-hydroxymuconic semialdehyde + H2O
?
show the reaction diagram
0.49% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00273
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
1.99
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
730
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
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?
Q84II3_JANS3
Janthinobacterium sp. (strain J3)
290
0
32300
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
2 * 33000, SDS-PAGE
70000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 33000, SDS-PAGE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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