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Information on EC 1.14.13.23 - 3-hydroxybenzoate 4-monooxygenase
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1.14.13.23 3-hydroxybenzoate 4-monooxygenaseIUBMB Comments
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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Word Map
- 1.14.13.23
- 4-hydroxybenzoate
- testosteroni
- phenol
- fad
-
comamonas
- hydroxylases
- gentisate
-
mobility-shift
-
unbound
- repressor
- mobr
- dioxygenase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3-hydroxybenzoate 4-hydroxylase, 3-hydroxybenzoate hydroxylase, 3-hydroxybenzoate-4-hydroxylase, EC 1.14.99.13, m-hydroxybenzoate hydroxylase, MHBH, MobA, oxygenase, 3-hydroxybenzoate 4-mono-, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxybenzoate 4-hydroxylase
3-hydroxybenzoate hydroxylase
3-hydroxybenzoate-4-hydroxylase
EC 1.14.99.13
-
-
formerly
-
m-hydroxybenzoate hydroxylase
MHBH
MobA
oxygenase, 3-hydroxybenzoate 4-mono-
-
-
-
-
3-hydroxybenzoate 4-hydroxylase
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-
-
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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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-
-
-
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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-
-
-
redox reaction
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-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
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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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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
low activity
i.e. procatechuate
-
?
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
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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
-
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
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-
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
-
-
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
-
i.e. procatechuate
-
?
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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-
-
-
?
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
?
-
-
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
?
-
-
the enzyme has a large tunnel for substrate and oxygen access to the active site
-
-
?
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NATURAL SUBSTRATE
NATURAL 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 + 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
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 + [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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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxy-3-iodomethylbenzoate
-
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
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
-
the enzyme is specifically induced by 3-hydroxybenzoate, no activation by 4-hydroxybenzoate
-
additional information
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
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the aerobic soil bacterium that utilizes 3-hydroxybenzoate as a sole carbon and energy source
brenda
additional information
-
the aerobic soil bacterium that utilizes 3-hydroxybenzoate as a sole carbon and energy source
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate
metabolism
-
the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A6N4XUQ0_9FLAO
485
1
54782
TrEMBL
-
A0A6N4X377_9FLAO
485
1
54890
TrEMBL
-
A0A2R8BDQ6_9RHOB
644
0
71778
TrEMBL
-
A0A645DRE1_9ZZZZ
81
0
9005
TrEMBL
other Location (Reliability: 2)
A0A221K1H5_9RHOB
622
0
67512
TrEMBL
-
A0A499Q469_CHRMO
335
0
37957
TrEMBL
other Location (Reliability: 2)
A0A2R8B9R4_9RHOB
615
0
67957
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
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
-
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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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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brenda
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