We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase, dhb dehydrogenase, dihydrodihydroxybenzoate dehydrogenase, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-dihydroxycyclohexa-3,5-diene dehydrogenase
-
-
-
-
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
-
-
-
-
2-hydro-1,2-dihydroxybenzoate dehydrogenase
-
-
-
-
3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase
-
-
-
-
3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase
-
-
-
-
cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase
-
-
-
-
cis-Diol dehydrogenase (Acinetobacter calcoaceticus reduced)
-
-
-
-
cis-diol dehydrogenase (Pseudomonas putida reduced)
-
-
-
-
dehydrogenase 1,2-dihydro-1,2-dihydroxybenzoate (Acinetobacter strain ADP1 gene benD)
-
-
-
-
dehydrogenase, 1,2-dihydro-1,2-dihydroxybenzoate (Acinetobacter calcoaceticus strain ADP1 gene benD reduced)
-
-
-
-
dehydrogenase, 1,2-dihydro-1,2-dihydroxybenzoate (plasmid pWWO clone pPL392 gene xylL reduced)
-
-
-
-
dehydrogenase, 3,5-cyclohexadiene-1,2-diol-1-carboxylate
-
-
-
-
dihydrodihydroxybenzoate dehydrogenase
-
-
-
-
EC 1.3.1.55
-
-
formerly
-
GenBank AF009224-derived protein GI 2996624
-
-
-
-
DHB dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
mechanism
-
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
mechanism
-
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
by growth on 3-chloro-, 4-chloro-, and 3,5-dichlorobenzoate enzyme is induced when combinated with recombinant toluate-1,2-dioxygenase
-
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
by growth on 3-chloro-, 4-chloro-, and 3,5-dichlorobenzoate enzyme is induced when combinated with recombinant toluate-1,2-dioxygenase
-
-
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
mechanism
-
-
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
146888-19-9
formerly EC 1.3.1.55
146888-20-2
formerly EC 1.3.1.55
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
3-methyl-4,5-cyclohexadiene-cis-1,2-diol-1-carboxylic acid + NAD+
3-methylcatechol + CO2 + NADH
-
-
-
?
3-methyldihydrodihydroxybenzoate + NAD+
3-methylcatechol + CO2 + NADH
cis-1,2-cyclohexanediol + NAD+
?
-
at 95% of the activity with cis-benzene dihydrodiol
-
-
?
cis-benzene dihydrodiol + NAD+
dihydroxybenzene + NADH
additional information
?
-
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
enzyme in the pathway of dissimilation of benzoate via catechol
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
free carboxyl groups essential
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
enzyme is involved in the metabolism of benzene. A bedD mutant in which the gene is disrupted by a kanamycin resistance cassette is unable to utilize benzene for growth
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
free carboxyl groups essential
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
free carboxyl groups essential
-
?
1,2-propanediol + NAD+
?
-
at 189% of the activity with cis-benzene dihydrodiol
-
-
?
1,2-propanediol + NAD+
?
-
at 189% of the activity with cis-benzene dihydrodiol
-
-
?
3-methyldihydrodihydroxybenzoate + NAD+
3-methylcatechol + CO2 + NADH
-
assay substrate
-
-
?
3-methyldihydrodihydroxybenzoate + NAD+
3-methylcatechol + CO2 + NADH
-
assay substrate
-
-
?
cis-benzene dihydrodiol + NAD+
dihydroxybenzene + NADH
-
-
-
?
cis-benzene dihydrodiol + NAD+
dihydroxybenzene + NADH
-
-
-
-
?
cis-benzene dihydrodiol + NAD+
dihydroxybenzene + NADH
-
-
-
-
?
glycerol + NAD+
?
-
at 18% of the activity with cis-benzene dihydrodiol
-
-
?
glycerol + NAD+
?
-
at 18% of the activity with cis-benzene dihydrodiol
-
-
?
additional information
?
-
-
no substrates: benzoic acid, cis-3,5-cyclohexadien-1,2-diol
-
-
?
additional information
?
-
-
purified recombinant enzyme also shows methyl transfer activity, methyl group is transferred from 4-methyl-3,5-cyclohexadiene-cis-1,2-diol-1-carboxylic acid to 3-methyl, only in presence of adenosylcobalamin as methyl group acceptor
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
enzyme in the pathway of dissimilation of benzoate via catechol
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
free carboxyl groups essential
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
enzyme is involved in the metabolism of benzene. A bedD mutant in which the gene is disrupted by a kanamycin resistance cassette is unable to utilize benzene for growth
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
free carboxyl groups essential
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
-
-
-
?
(-)-3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+
catechol + CO2 + NADH
-
free carboxyl groups essential
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adenosylcobalamin
-
required as methyl acceptor for the methyl transfer activity of recombinant enzyme from E. coli
NAD+
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
m-toluate
-
recombinant in Rhodobacter sphaeroides
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.2
(-)-3,5-cyclohexadien-1,2-diol-1-carboxylate
-
-
0.286
cis-benzene dihydrodiol
-
-
additional information
additional information
-
0.0435
NAD+
-
-
additional information
additional information
-
dependency on pH
-
additional information
additional information
-
substituted substrates
-
additional information
additional information
-
substituted substrates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
wild-type enzyme, native and recombinant, and mutants, activity depending on growth substrates
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
basonym Alcaligenes eutrophus
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
wild-type ADP1 and spontaneous mutants ADP136, ADP137, ADP138
-
-
brenda
-
-
-
brenda
only TOL plasmid is mentioned, which is derived from Pseudomonas putida, but not Pseudomonas putida itself
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
24000
-
? * 24000, SDS-PAGE
28000
-
? * 28000, DNA sequence determination, recombinant from Escherichia coli
31000
-
2 * 31000, SDS-PAGE
94600
-
sedimentation equilibrium centrifugation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 31000, SDS-PAGE
?
-
? * 24000, SDS-PAGE
?
-
? * 28000, DNA sequence determination, recombinant from Escherichia coli
tetramer
-
4 * 110000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
operon insertion mutants of recombinant Escherichia coli expressing the TOL plasmid encoded enzymes including 1,2-dihydroxy--3,5-cyclohexadiene-1-carboxylate dehydrogenase, sequence analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50
-
native enzyme: 10 min, 90% activity, recombinant enzyme: 5 min, complete inactivation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
partial, recombinant from Escherichia coli and Acinetobacter calcoaceticus
-
recombinant from Escherichia coli
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
addition of recombinant enzyme on plasmid TOL plasmid of donor PaW1 to native one in B13 derivative WR1
-
expression of wild-type benD gene and native mutant genes in Escherichia coli and Acinetobacter calcoaceticus
-
expression of xylL gene in Escherichia coli strain from TOL plasmid
-
expression of xylL gene in Escherichia coli, plasmid hybrid pBR322 and pPl401
-
expression of xylL gene in Rhodobacter sphaeroides encoded on TOL plasmid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Neidle, E.; Hartnett, C.; Ornston, L.N.; Bairoch, A.; Rekik, M.; Harayama, S.
cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily
Eur. J. Biochem.
204
113-120
1992
Acinetobacter calcoaceticus
brenda
Fong, K.P.Y.; Goh, C.B.H.; Tan, H.M.
Characterization and expression of the plasmid-borne bedD gene from Pseudomonas putida ML2, which codes for a NAD+-dependent cis-benzene dihydrodiol dehydrogenase
J. Bacteriol.
178
5592-5601
1996
Pseudomonas putida, Pseudomonas putida ML2
brenda
Lee, J.Y.; Park, H.S.; Kim, H.S.
Adenosylcobalamin-mediated methyl transfer by toluate cis-dihydrodiol dehydrogenase of the TOL plasmid pWW0
J. Bacteriol.
181
2953-2957
1999
Pseudomonas sp., Pseudomonas putida
brenda
Neidle, E.L.; Shapiro, M.K.; Ornston, L.N.
Cloning and expression in Escherichia coli of Acinetobacter calcoaceticus genes for benzoate degradation
J. Bacteriol.
169
5496-5503
1987
Acinetobacter calcoaceticus
brenda
Lehrbach, P.R.; Zeyer, J.; Reineke, W.; Knackmuss, H.J.; Timmis, K.N.
Enzyme recruitment in vitro: use of cloned genes to extend the range of haloaromatics degraded by Pseudomonas sp. strain B13
J. Bacteriol.
158
1025-1032
1984
Pseudomonas putida
brenda
Reiner, A.M.
Metabolism of aromatic compounds in bacteria. Purification and properties of the catechol-forming enzyme, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (NAD +) oxidoreductase (decarboxylating)
J. Biol. Chem.
247
4960-4965
1972
Cupriavidus necator
brenda
Harayama, S.; Rekik, M.
The meta cleavage operon of TOL degradative plasmid pWW0 comprises 13 genes
Mol. Gen. Genet.
221
113-120
1990
Pseudomonas putida
brenda
Reineke, W.; Knackmuss, H.J.
Hybrid pathway for chlorobenzoate metabolism in Pseudomonas sp. B13 derivatives
J. Bacteriol.
142
467-473
1980
Pseudomonas sp., Pseudomonas sp. B13
brenda
Zeyer, J.; Lehrbach, P.R.; Timmis, K.N.
Use of cloned genes of Pseudomonas TOL plasmid to effect biotransformation of benzoates to cis-dihydrodiols and catechols by Escherichia coli cells
Appl. Environ. Microbiol.
50
1409-1413
1985
Pseudomonas putida
brenda
Calero, S.; Gari, E.; Gibert, I.; Barbe, J.
Expression of the meta-cleavage pathway operon of the TOL plasmid of Pseudomonas putida in the phototrophic bacterium Rhodobacter sphaeroides
J. Biotechnol.
12
231-246
1989
Pseudomonas putida
-
brenda
Reineke, W.; Knackmuss, H.J.
Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on dehydrogenation of 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid
Biochim. Biophys. Acta
542
424-429
1978
Cupriavidus necator, Pseudomonas sp., Pseudomonas sp. B13
brenda
Mason, J.R.; Geary, P.J.
cis-1,2-Dihydroxycyclohexa-3,5-diene (NAD) oxidoreductase cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida NCIB 12190
Methods Enzymol.
23
134-137
1990
Pseudomonas putida, Pseudomonas putida NCIB12190
-
brenda
Select items on the left to see more content.
html completed
1.3.1.25 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
more
top
