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Enzyme Nomenclature
Information on EC 1.14.13.23 - 3-hydroxybenzoate 4-monooxygenase
for references in articles please use BRENDA:EC1.14.13.23
Word Map on EC 1.14.13.23
- 1.14.13.23
- testosteroni
- phenol
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comamonas
- fad
-
hydroxylases
- 4-hydroxybenzoate
-
unbound
- gentisate
-
mobility-shift
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.14.13.23
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybenzoate 4-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
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-
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37256-76-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
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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-
-
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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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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low activity
i.e. procatechuate
-
?
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
-
-
?
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
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
-
-
-
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
xenon
binding structure of xenon atoms, crystal structure, overview
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxy-3-iodomethylbenzoate
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inhibition not 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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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
NADPH
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cosubstrates 3-hydroxyanthranilate or 3,5-dihydroxybenzoate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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the aerobic soil bacterium that utilizes 3-hydroxybenzoate as a sole carbon and energy source
additional information
-
the aerobic soil bacterium that utilizes 3-hydroxybenzoate as a sole carbon and energy source
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
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
-
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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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.23)
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