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Information on EC 1.14.13.23 - 3-hydroxybenzoate 4-monooxygenase for references in articles please use BRENDA:EC1.14.13.23Word Map on EC 1.14.13.23
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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3-hydroxybenzoate 4-monooxygenase
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3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
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3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
structural variations in the catalytic action, reaction mechanism
3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
structural variations in the catalytic action, reaction mechanism
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Polycyclic aromatic hydrocarbon degradation
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Microbial metabolism in diverse environments
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3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating)
A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
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3-hydroxybenzoate 4-hydroxylase
3-hydroxybenzoate hydroxylase
3-hydroxybenzoate-4-hydroxylase
EC 1.14.99.13
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formerly
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m-hydroxybenzoate hydroxylase
oxygenase, 3-hydroxybenzoate 4-mono-
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3-hydroxybenzoate 4-hydroxylase
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3-hydroxybenzoate 4-hydroxylase
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3-hydroxybenzoate 4-hydroxylase
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3-hydroxybenzoate hydroxylase
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3-hydroxybenzoate hydroxylase
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3-hydroxybenzoate hydroxylase
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3-hydroxybenzoate hydroxylase
;
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3-hydroxybenzoate-4-hydroxylase
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3-hydroxybenzoate-4-hydroxylase
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m-hydroxybenzoate hydroxylase
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m-hydroxybenzoate hydroxylase
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MHBH
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MobA
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brenda
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SwissProt
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gene mobA
SwissProt
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SwissProt
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gene mobA
SwissProt
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metabolism
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the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate
metabolism
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the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate
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2,3-dihydroxybenzoate + NADPH + O2
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2,5-dihydroxybenzoate + NADPH + O2
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2-fluoro-5-hydroxybenzoate + NADPH + O2
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3,5-dihydroxybenzoate + NADPH + O2
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3-hydroxyanthranilate + NADPH + O2
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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-fluoro-3-hydroxybenzoate + NADPH + O2
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4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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low activity
i.e. procatechuate
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gentisate + NADPH + O2
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additional information
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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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
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
substrate recognition and substrate-binding site structure and involved residues, overview
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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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
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
substrate recognition and substrate-binding site structure and involved residues, overview
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3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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i.e. procatechuate
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3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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additional information
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the enzyme has a large tunnel for substrate and oxygen access to the active site
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additional information
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the enzyme has a large tunnel for substrate and oxygen access to the active site
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additional information
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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
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i.e. procatechuate
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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
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low activity
i.e. procatechuate
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Q6SSJ6
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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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
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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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
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3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Q6SSJ6
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3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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NADH
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poor substitute for NADPH
FAD
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flavoprotein
FAD
binding site structure
NADPH
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NADPH
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specific requirement for NADPH
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xenon
binding structure of xenon atoms, crystal structure, overview
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4-chloromercuribenzoate
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4-hydroxy-3-iodomethylbenzoate
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inhibition not reversed in presence of dithiotreitol
diethyldithiocarbamate
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iodoacetamide
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inhibition reversed in presence of dithiotreitol
MobR
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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
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N-iodosuccinimide
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inhibition reversed in presence of dithiotreitol
o-Iodosobenzoate
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inhibition reversed in presence of dithiotreitol
p-hydroxymercuribenzoate
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additional information
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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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additional information
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the enzyme is specifically induced by 3-hydroxybenzoate, no activation by 4-hydroxybenzoate
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additional information
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3-hydroxybenzoate binds to the transcriptional regulator MobR as a ligand, resulting in an efficient induction of gene mobA, that encodes a 3-hydroxybenzoate 4-hydroxylase
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0.06
2,3-Dihydroxybenzoate
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cosubstrate NADPH
0.5
2,5-Dihydroxybenzoate
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cosubstrate NADPH
0.04
3,5-Dihydroxybenzoate
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cosubstrate NADPH
0.03 - 0.19
3-hydroxybenzoate
0.12
4-Fluoro-3-hydroxybenzoate
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cosubstrate NADPH
0.03
m-Hydroxybenzoate
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3
NADH
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cosubstrate 3-hydroxybenzoate
0.03
3-hydroxybenzoate
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cosubstrate NADPH
0.19
3-hydroxybenzoate
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0.02
NADPH
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+ 2-fluoro-5-hydroxybenzoate
0.05
NADPH
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cosubstrates 3-hydroxyanthranilate or 3,5-dihydroxybenzoate
0.07
NADPH
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cosubstrates 3-hydroxybenzoate or 2,3-dihydroxybenzoate
0.14
NADPH
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+ 2,5-dihydroxybenzoate
0.15
NADPH
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+ 4-fluoro-3-hydroxybenzoate
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0.002
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uninduced wild-type strain
0.055
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wild-type strain induced by 3-hydroxybenzoate
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6.2
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in potassium phosphate buffer
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30
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assay at
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additional information
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the aerobic soil bacterium that utilizes 3-hydroxybenzoate as a sole carbon and energy source
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additional information
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the aerobic soil bacterium that utilizes 3-hydroxybenzoate as a sole carbon and energy source
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71000
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x * 71000, SDS-PAGE
145000
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sedimentation equilibrium centrifugation
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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
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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
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additional information
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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
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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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1.4-1.6 M ammonium sulfate, 4-8% dioxane, pH 6.5
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purified native enzyme in complex with substrate 3-hydroxybenzoate or inhibitor 4-chloromercuribenzoate, and as Xe-derivative, sitting drop vapour diffusion method, 10 mg/ml in 25 mM phosphate buffer, pH 7.5, containing 0.3 mM 3-hydroxybenzoate, mixed with an equal volume of a reservoir solution consisting of 0.1 M MES, pH 6.5, 1.3 M ammonium sulfate, and 6% v/v 1,4-dioxane, 20°C, X-ray diffraction structure determination and analysis at 1.8 A and 2.5 A resolution, respectively
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2-mercaptoethanol stabilizes
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DNA and amino acid sequence determination and analysis, sequence comparisons
gene mobA, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli
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gene mobA, promoter study, primer extension method, transription regulation/repression by MobR, genetic organization, overview, overexpression of mobA and of a mobA-mobR fusion construct in Escherichia coli
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A400G
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random mutagenesis, the substitution confers the ability to the mutant enzyme to transform 3-aminophenol to a related substituted catechol
D416A
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random mutagenesis, the substitution confers the ability to the mutant enzyme to transform 3-aminophenol to a related substituted catechol
H135P
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random mutagenesis, the substitution confers the ability to the mutant enzyme to transform 3-aminophenol to a related substituted catechol
K326I
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random mutagenesis, the substitution confers the ability to the mutant enzyme to transform phenol to catechol
V257A
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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
additional information
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screening of random mutants from a cosmid library for altered substrate specificities
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MOBA_COMTE
639
70489
Swiss-Prot
A0A1K2FZL8_9ACTN
624
68473
TrEMBL
A0A2R8B9R4_9RHOB
615
67957
TrEMBL
A0A2R8BDQ6_9RHOB
644
71778
TrEMBL
A0A2R8CHR2_9GAMM
625
69360
TrEMBL
A0A2R8B0D2_9RHOB
642
71235
TrEMBL
A0A221K1H5_9RHOB
622
67512
TrEMBL
A0A143QMU4_9NOCA
641
70319
TrEMBL
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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
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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
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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
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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, Comamonas testosteroni (Q6SSJ6), Comamonas testosteroni KH122-3s, Comamonas testosteroni KH122-3s (Q6SSJ6)
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, Comamonas testosteroni KH122-3s (Q6SSJ6)
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
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brenda
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