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2-methylbenzoate + O2 + NADH
cis-1,2-dihydro-1,2-dihydroxy-2-methyl-benzoate + NAD+
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
4-fluorobenzoate + O2 + NADH
4-fluoro-2-hydro-1,2-dihydroxybenzoate
benzene + NADH + H+ + O2
?
benzene + O2 + NADH
(R,S)-1,2-dihydro-1,2-dihydroxycatechol + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
benzoate + NADH + H+ + O2
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
benzoate + NADH-cytochrome c reductase component + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+-cytochrome c reductase component
-
-
-
-
r
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
butyl benzol + NADH + H+ + O2
?
ethyl benzene + NADH + H+ + O2
?
additional information
?
-
2-methylbenzoate + O2 + NADH
cis-1,2-dihydro-1,2-dihydroxy-2-methyl-benzoate + NAD+
-
-
-
-
?
2-methylbenzoate + O2 + NADH
cis-1,2-dihydro-1,2-dihydroxy-2-methyl-benzoate + NAD+
-
-
-
-
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
-
-
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
-
-
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
-
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
-
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
benzoate analogues with substituents in meta position are oxygenated more rapidly than those with ortho- or para substitution
-
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
benzoate analogues with substituents in meta position are oxygenated more rapidly than those with ortho- or para substitution
-
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
-
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
-
?
4-fluorobenzoate + O2 + NADH
4-fluoro-2-hydro-1,2-dihydroxybenzoate
-
-
-
?
4-fluorobenzoate + O2 + NADH
4-fluoro-2-hydro-1,2-dihydroxybenzoate
-
-
-
?
benzene + NADH + H+ + O2
?
-
-
-
-
?
benzene + NADH + H+ + O2
?
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
?
-
-
-
-
?
benzoate + NADH + H+ + O2
?
-
-
-
-
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
-
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
catabolism of aromatic compounds
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
catabolism of aromatic compounds
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
-
-
?
butyl benzol + NADH + H+ + O2
?
-
-
-
-
?
butyl benzol + NADH + H+ + O2
?
-
-
-
-
?
ethyl benzene + NADH + H+ + O2
?
-
highest activity
-
-
?
ethyl benzene + NADH + H+ + O2
?
-
highest activity
-
-
?
additional information
?
-
-
benzoate induces the expression of benzoate 1,2-dioxygenase
-
-
?
additional information
?
-
-
benzoate 1,2 dioxygenase oxygenase component (BZDO) prepared in a form with the Rieske cluster oxidized and the mononuclear iron in the Fe(III) state can utilize H2O2 as a source of reduced oxygen to form the correct cis-dihydrodiol product from benzoate
-
-
?
additional information
?
-
-
benzoate 1,2 dioxygenase oxygenase component (BZDO) prepared in a form with the Rieske cluster oxidized and the mononuclear iron in the Fe(III) state can utilize H2O2 as a source of reduced oxygen to form the correct cis-dihydrodiol product from benzoate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
additional information
?
-
-
benzoate induces the expression of benzoate 1,2-dioxygenase
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
-
-
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
-
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
-
Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
catabolism of aromatic compounds
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
catabolism of aromatic compounds
-
-
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
-
-
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + 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.
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.
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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.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Yamaguchi, M.; Fujisawa, H.
Purification and characterization of an oxygenase component in benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1
J. Biol. Chem.
255
5058-5063
1980
Pseudomonas putida, Pseudomonas putida C-1
brenda
Yamaguchi, M.; Fujisawa, H.
Subunit structure of oxygenase component in benzoate-1,2-dioxygenase system from Pseudomonas arvilla C-1
J. Biol. Chem.
257
12497-12502
1982
Pseudomonas putida, Pseudomonas putida C-1
brenda
Bundy, B.M.; Campbell, A.L.; Neidle, E.L.
Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1
J. Bacteriol.
180
4466-4474
1998
Acinetobacter sp., Acinetobacter sp. ADP1
brenda
Haddad, S.; Eby, D.M.; Neidle, E.L.
Cloning and expression of the benzoate dioxygenase genes from Rhodococcus sp. strain 19070
Appl. Environ. Microbiol.
67
2507-2514
2001
Rhodococcus sp., Rhodococcus sp. 19070
brenda
Wolfe, M.D.; Altier, D.J.; Stubna, A.; Popescu, C.V.; Muenck, E.; Lipscomb, J.D.
Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a two-component Rieske dioxygenase
Biochemistry
41
9611-9626
2002
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
brenda
Xu, Y.; Chen, M.; Zhang, W.; Lin, M.
Genetic organization of genes encoding phenol hydroxylase, benzoate 1,2-dioxygenase alpha subunit and its regulatory proteins in Acinetobacter calcoaceticus PHEA-2
Curr. Microbiol.
46
235-240
2003
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus PHEA-2
brenda
Ge, Y.; Eltis, L.D.
Characterization of hybrid toluate and benzoate dioxygenases
J. Bacteriol.
185
5333-5341
2003
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus BADO ADP1
brenda
Crosby, J.
Synthesis of optically active compounds: A large scale perspective
Tetrahedron
47
4789-4846
1991
Pseudomonas putida
-
brenda
Kim, Y.H.; Cho, K.; Yun, S.H.; Kim, J.Y.; Kwon, K.H.; Yoo, J.S.; Kim, S.I.
Analysis of aromatic catabolic pathways in Pseudomonas putida KT 2440 using a combined proteomic approach: 2-DE/MS and cleavable isotope-coded affinity tag analysis
Proteomics
6
1301-1318
2006
Pseudomonas putida, Pseudomonas putida KT 2440
brenda
Neibergall, M.B.; Stubna, A.; Mekmouche, Y.; Muenck, E.; Lipscomb, J.D.
Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase
Biochemistry
46
8004-8016
2007
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
brenda
Kim, D.; Kim, S.W.; Choi, K.Y.; Lee, J.S.; Kim, E.
Molecular cloning and functional characterization of the genes encoding benzoate and p-hydroxybenzoate degradation by the halophilic Chromohalobacter sp. strain HS-2
FEMS Microbiol. Lett.
280
235-241
2008
Chromohalobacter sp.
brenda
Sun, S.Y.; Zhang, X.; Zhou, Q.; Chen, J.C.; Chen, G.Q.
Microbial production of cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate by genetically modified Pseudomonas putida
Appl. Microbiol. Biotechnol.
80
977-984
2008
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Karandikar, R.; Badri, A.; Phale, P.S.
Biochemical characterization of inducible reductase component of benzoate dioxygenase and phthalate isomer dioxygenases from Pseudomonas aeruginosa strain PP4
Appl. Biochem. Biotechnol.
177
318-333
2015
Pseudomonas aeruginosa, Pseudomonas aeruginosa PP4
brenda
Rivard, B.S.; Rogers, M.S.; Marell, D.J.; Neibergall, M.B.; Chakrabarty, S.; Cramer, C.J.; Lipscomb, J.D.
Rate-determining attack on substrate precedes rieske cluster oxidation during cis-dihydroxylation by benzoate dioxygenase
Biochemistry
54
4652-4664
2015
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
brenda
Solyanikova, I.P.; Borzova, O.V.; Emelyanova, E.V.
Kinetics of interaction between substrates/substrate analogs and benzoate 1,2-dioxygenase from benzoate-degrading Rhodococcus opacus 1CP
Folia Microbiol. (Praha)
62
355-362
2017
Rhodococcus opacus, Rhodococcus opacus 1CP
brenda
Tavakoli, A.; Hamzah, A.; Rabu, A.
Expression, purification and kinetic characterization of recombinant benzoate dioxygenase from Rhodococcus ruber UKMP-5M
Mol. Biol. Res. Commun.
5
133-142
2016
Rhodococcus ruber, Rhodococcus ruber UKMP-5M
brenda