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2,3-dihydroxybenzoate + NADPH + O2
?
-
-
-
-
?
2,5-dihydroxybenzoate + NADPH + O2
?
-
-
-
-
?
2-fluoro-5-hydroxybenzoate + NADPH + O2
?
-
-
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
?
-
-
-
-
?
3-hydroxyanthranilate + NADPH + O2
?
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
4-fluoro-3-hydroxybenzoate + NADPH + O2
?
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
low activity
i.e. procatechuate
-
?
gentisate + NADPH + O2
?
-
-
-
-
?
additional information
?
-
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
initial step of the degradation in the meta-cleavage pathway leading to tricarboxylic acid cycle intermediates, MobR negatively regulates the expression of mobA, the repression is relieved by binding of 3-hydroxybenzoate
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
substrate recognition and substrate-binding site structure and involved residues, overview
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
initial step of the degradation in the meta-cleavage pathway leading to tricarboxylic acid cycle intermediates, MobR negatively regulates the expression of mobA, the repression is relieved by binding of 3-hydroxybenzoate
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
substrate recognition and substrate-binding site structure and involved residues, overview
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
r
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
i.e. procatechuate
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
the enzyme has a large tunnel for substrate and oxygen access to the active site
-
-
?
additional information
?
-
-
the enzyme has a large tunnel for substrate and oxygen access to the active site
-
-
?
additional information
?
-
enzyme 3HB4H catalyzes an ortho-hydroxylation reaction
-
-
-
additional information
?
-
the enzyme has a large tunnel for substrate and oxygen access to the active site
-
-
?
additional information
?
-
-
the enzyme has a large tunnel for substrate and oxygen access to the active site
-
-
?
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
low activity
i.e. procatechuate
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
initial step of the degradation in the meta-cleavage pathway leading to tricarboxylic acid cycle intermediates, MobR negatively regulates the expression of mobA, the repression is relieved by binding of 3-hydroxybenzoate
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
initial step of the degradation in the meta-cleavage pathway leading to tricarboxylic acid cycle intermediates, MobR negatively regulates the expression of mobA, the repression is relieved by binding of 3-hydroxybenzoate
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
i.e. procatechuate
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
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4-chloromercuribenzoate
-
4-hydroxy-3-iodomethylbenzoate
-
inhibition not reversed in presence of dithiotreitol
diethyldithiocarbamate
-
-
iodoacetamide
-
inhibition reversed in presence of dithiotreitol
MobR
-
a 42 kDa dimeric transcriptional regulator of the MarR family, encoded by an open reading frame mobR in the upstream region of mobA, binds to the target DNA and negatively regulates the expression of mobA, the repression is relieved by binding of 3-hydroxybenzoate, binding kinetics, overview
-
N-iodosuccinimide
-
inhibition reversed in presence of dithiotreitol
o-Iodosobenzoate
-
inhibition reversed in presence of dithiotreitol
p-hydroxymercuribenzoate
-
-
additional information
MobR from Comamonas testosteroni KH122-3s is a member of the MarR family of transcriptional regulators, binds to DNA, and functions as a repressor for the mobA gene, that encodes a 3-hydroxybenzoate 4-hydroxylase, MobR is inactivated at a high concentration of 2,5-dihydroxybenzoate, 2,3-dihydroxybenzoate, 3-hydroxybenzoate and 3,5-dihydroxybenzoate
-
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dimer
the enzyme forms an active homodimer with crystallographic 2-fold symmetry, in which each subunit consists of the first two domains comprising an active site and the C-terminal domain involved in oligomerization
dimer
-
the enzyme forms an active homodimer with crystallographic 2-fold symmetry, in which each subunit consists of the first two domains comprising an active site and the C-terminal domain involved in oligomerization
-
additional information
the enzyme has a large tunnel, connecting the substrate binding pocket to the protein surface, for substrate and oxygen access to the active site, fold of the catalytic domain and the active-site architecture, including the FAD and substrate-binding sites, overview
additional information
-
the enzyme has a large tunnel, connecting the substrate binding pocket to the protein surface, for substrate and oxygen access to the active site, fold of the catalytic domain and the active-site architecture, including the FAD and substrate-binding sites, overview
additional information
-
the enzyme has a large tunnel, connecting the substrate binding pocket to the protein surface, for substrate and oxygen access to the active site, fold of the catalytic domain and the active-site architecture, including the FAD and substrate-binding sites, overview
-
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A400G
random mutagenesis, the substitution confers the ability to the mutant enzyme to transform 3-aminophenol to a related substituted catechol
D416A
random mutagenesis, the substitution confers the ability to the mutant enzyme to transform 3-aminophenol to a related substituted catechol
H135P
random mutagenesis, the substitution confers the ability to the mutant enzyme to transform 3-aminophenol to a related substituted catechol
K326I
random mutagenesis, the substitution confers the ability to the mutant enzyme to transform phenol to catechol
additional information
screening of random mutants from a cosmid library for altered substrate specificities
V257A
random mutagenesis, the substitution confers the ability to the mutant enzyme to transform phenol to catechol, the mutant is also active with resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol
V257A
a directed evolution study reveals that 3HB4H from Comamonas testosteroni strain GZ39 is considerably active with 4-hydroxybenzoate and that this activity increases in the V257A variant. The same variant slowly converts phenol to catechol, an activity not observed with the wild-type enzyme
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Chen, R.; Oki, H.; Scott, R.P.; Yamaguchi, H.; Kusunoki, M.; Matsuura, Y.; Chaen, H.; Tsugita, A.; Hosokawa, K.
Crystallization and further characterization of meta-hydroxybenzoate 4-hydroxylase from Comamonas testosteroni
Res. Commun. Biochem. Cell Mol. Biol.
2
253-274
1998
Comamonas testosteroni
-
brenda
Michalover, J.M.; Ribbons, D.W.
3-Hydroxybenzoate 4-hydroxylase from Pseudomonas testosteroni
Biochem. Biophys. Res. Commun.
55
888-896
1973
Comamonas testosteroni
brenda
Kumar, R.P.; Rao, P.V.S.; Vaidyanathan, C.S.
m-Hydroxybenzoate 4-hydroxylase from Aspergillus niger: purification and properties
Indian J. Biochem. Biophys.
10
184-190
1973
Aspergillus niger
brenda
Mashetty, S.B.; Manohar, S.; Karegoudar, T.B.
Degradation of 3-hydroxybenzoic acid by a Bacillus species
Indian J. Biochem. Biophys.
33
145-148
1996
Bacillus sp. (in: Bacteria)
brenda
Chen, R.; Oki, H.; Chaen, H.; Hosokawa, K.
Studies on m-hydroxybenzoate 4-hydroxylase from Comamonas testosteroni I. Purification and characterization
Res. Commun. Biochem. Cell Mol. Biol.
1
304-322
1997
Comamonas testosteroni
-
brenda
Hiromoto, T.; Matsue, H.; Yoshida, M.; Tanaka, T.; Higashibata, H.; Hosokawa, K.; Yamaguchi, H.; Fujiwara, S.
Characterization of MobR, the 3-hydroxybenzoate-responsive transcriptional regulator for the 3-hydroxybenzoate hydroxylase gene of Comamonas testosteroni KH122-3s
J. Mol. Biol.
364
863-877
2006
Comamonas testosteroni, Comamonas testosteroni KH122-3s
brenda
Hiromoto, T.; Fujiwara, S.; Hosokawa, K.; Yamaguchi, H.
Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site
J. Mol. Biol.
364
878-896
2006
Comamonas testosteroni (Q6SSJ6), Comamonas testosteroni, Comamonas testosteroni KH122-3s (Q6SSJ6), Comamonas testosteroni KH122-3s
brenda
Yoshida, M.; Hiromoto, T.; Hosokawa, K.; Yamaguchi, H.; Fujiwara, S.
Ligand specificity of MobR, a transcriptional regulator for the 3-hydroxybenzoate hydroxylase gene of Comamonas testosteroni KH122-3s
Biochem. Biophys. Res. Commun.
362
275-280
2007
Comamonas testosteroni (Q6SSJ6), Comamonas testosteroni KH122-3s (Q6SSJ6), Comamonas testosteroni KH122-3s
brenda
Chang, H.K.; Zylstra, G.J.
Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase
Biochem. Biophys. Res. Commun.
371
149-153
2008
Comamonas testosteroni (Q6SSJ6)
brenda
Mulla, S.; Bangeppagari, M.; Mahadevan, G.; Eqani, S.; Sajjan, D.; Tallur, P.; Megadi, V.; Ninnekar, H.
Biodegradation of 3-chlorobenzoate and 3-hydroxybenzoate by polyurethane foam immobilized cells of Bacillus sp. OS13
J. Environ. Chem. Eng.
4
1423-1431
2016
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OS13
-
brenda
Westphal, A.H.; Tischler, D.; van Berkel, W.J.H.
Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases
Arch. Biochem. Biophys.
702
108820
2021
Comamonas testosteroni (Q6SSJ6)
brenda