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Information on EC 1.14.13.23 - 3-hydroxybenzoate 4-monooxygenase
for references in articles please use BRENDA:EC1.14.13.23
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.23 3-hydroxybenzoate 4-monooxygenase
IUBMB Comments
A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.14.13.23
- phenol
- 4-hydroxybenzoate
- hydroxylases
- testosteroni
- fad
- gentisate
-
comamonas
-
mobility-shift
- salicylate
- repressor
-
regioselective
- flavoprotein
-
unbound
- mobr
- dioxygenase
- protocatechuate
showSynonyms
3-hydroxybenzoate hydroxylase, 3-hydroxybenzoate 4-hydroxylase, 3-hydroxybenzoate-4-hydroxylase, 3-hydroxybenzoate 4-monooxygenase, more
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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
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m-hydroxybenzoate hydroxylase
MHBH
MobA
oxygenase, 3-hydroxybenzoate 4-mono-
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-
-
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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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-
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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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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
m-cresol degradation
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybenzoate + NADPH + O2
?
-
Substrates: -
Products: -
Products: -
?
2-fluoro-5-hydroxybenzoate + NADPH + O2
?
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
4-fluoro-3-hydroxybenzoate + NADPH + O2
?
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
Substrates: low activity
Products: i.e. procatechuate
Products: i.e. procatechuate
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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Substrates: 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
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Substrates: substrate recognition and substrate-binding site structure and involved residues, overview
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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Substrates: 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
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Substrates: substrate recognition and substrate-binding site structure and involved residues, overview
Products: -
Products: -
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
r
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
Substrates: -
Products: i.e. procatechuate
Products: i.e. procatechuate
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
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Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has a large tunnel for substrate and oxygen access to the active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has a large tunnel for substrate and oxygen access to the active site
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme 3HB4H catalyzes an ortho-hydroxylation reaction
Products: -
Products: -
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additional information
?
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Substrates: the enzyme has a large tunnel for substrate and oxygen access to the active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has a large tunnel for substrate and oxygen access to the active site
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: low activity
Products: i.e. procatechuate
Products: i.e. procatechuate
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
Substrates: 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
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
Substrates: 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
Products: -
Products: -
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
Substrates: -
Products: i.e. procatechuate
Products: i.e. procatechuate
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
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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
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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
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phylogenetic analysis of FAD-dependent 4-hydroxybenzoate hydroxylases and 3-hydroxybenzoate 4-hydroxylase, phylogenetic analysis and tree, overview. Enzyme structure analysis and comparisons (PDB ID pdb: 2dkh). Enzyme 3HB4H is missing a flexible loop, which is involved in flavin movement and closing-off the active site. In 3HB4H, the conserved tyrosine 222 makes a hydrogen bond with the hydroxyl group of the phenolic substrate, substrate binding pocket and structure-function analysis, homology modeling, overview. Residues Asp75 and Tyr271 might enhance the electron donating capacity of the hydroxyl group of 3-hydroxybenzoate (3-HB). The carboxyl group of 3-HB preferentially interacts with the side chains of His135 and Lys247. This ionic interaction is proposed to determine the orientation of bound substrate
metabolism
additional information
FAD-dependent hydroxybenzoate hydroxylase enzymes structure comparisons, overview
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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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). A0A645DRE1_9ZZZZ
81
0
9005
TrEMBL
other Location (Reliability: 2)
A0A2R8B0D2_9RHOB
642
0
71235
TrEMBL
-
A0A2R8B9R4_9RHOB
615
0
67957
TrEMBL
-
A0A499Q469_CHRMO
335
0
37957
TrEMBL
other Location (Reliability: 2)
A0A221K1H5_9RHOB
622
0
67512
TrEMBL
-
A0A2R8BDQ6_9RHOB
644
0
71778
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
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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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