Information on EC 1.14.13.23 - 3-hydroxybenzoate 4-monooxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.13.23
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxybenzoate 4-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
m-cresol degradation
-
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Benzoate degradation
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Polycyclic aromatic hydrocarbon degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-76-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2,5-dihydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-fluoro-5-hydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
3-hydroxyanthranilate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
-
i.e. procatechuate
-
?
3-hydroxybenzoate + NADPH + O2
3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
4-fluoro-3-hydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
low activity
i.e. procatechuate
-
?
gentisate + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
Q6SSJ6
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i.e. procatechuate
-
?
3-hydroxybenzoate + NADPH + O2
3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
show the reaction diagram
Q6SSJ6
low activity
i.e. procatechuate
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
poor substitute for NADPH
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
xenon
binding structure of xenon atoms, crystal structure, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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Heavy metal ions
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-
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iodoacetamide
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inhibition reversed in presence of dithiotreitol
m-Aminobenzoate
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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-ethylmaleimide
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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
o-phenanthroline
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p-hydroxymercuribenzoate
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Salicylaldoxime
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-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.02 - 0.2
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
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uninduced wild-type strain
0.01
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0.055
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wild-type strain induced by 3-hydroxybenzoate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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in potassium phosphate buffer
7.3
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in Tris-HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
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sedimentation equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 71000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
additional information
screening of random mutants from a cosmid library for altered substrate specificities