Information on EC 1.14.13.33 - 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.33
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RECOMMENDED NAME
GeneOntology No.
4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxybenzoate + NAD(P)H + H+ + O2 = 3,4-dihydroxybenzoate + NAD(P)+ + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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
Benzoate degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD). The enzyme from Corynebacterium cyclohexanicum is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at approximately equal rates (cf. EC 1.14.13.2 4-hydroxybenzoate 3-monooxygenase). It is less specific for NADPH than EC 1.14.13.2.
CAS REGISTRY NUMBER
COMMENTARY hide
95471-33-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PB4
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Manually annotated by BRENDA team
strain PB4
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Manually annotated by BRENDA team
no activity in Ralstonia paucula
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Manually annotated by BRENDA team
strain JJ-1b
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Manually annotated by BRENDA team
strain JJ-1b
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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
4-hydroxybenzoate + NAD(P)H + O2
3,4-dihydroxybenzoate + NAD(P)+ + H2O
show the reaction diagram
4-hydroxybenzoate + NAD(P)H + O2
protocatechuate + NAD(P)+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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flavoprotein, 0.8 FAD per enzyme molecule
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required for full activity in low concentrations of phosphate buffer, most effective at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dihydroxybenzoate
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over 70% inhibition at 10 mM
2,5-Dihydroxybenzoate
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over 70% inhibition at 10 mM
2-Hydroxybenzoate
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over 70% inhibition at 10 mM
3-hydroxybenzoate
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4-Aminobenzoate
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over 70% inhibition at 10 mM
4-Fluorobenzoate
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Cl-
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non-competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
4-hydroxybenzoate
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0.045
NADH
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pH 7.0-8.4
0.063 - 0.17
NADPH
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Km increases as pH rises from 7.0 to 8.4
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029 - 0.045
Cl-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.12
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crude cell extract
0.36
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for 4-hydroxybenzoate in the presence of NADPH
0.47
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for 4-hydroxybenzoate in the presence of NADH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.8
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pH 6.2: about 50% of activity maximum, pH 8.8: about 70% of activity maximum, NADPH
6.5 - 8.8
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50% of activity maximum at pH 6.5 and pH 8.8, NADH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
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PAGE of native and denatured enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 47000, PAGE of native and denatured enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 8.5
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4°C, 24 h, stable
438880
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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rapid inactivation above, p-hydroxybenzoate protects against heat inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
praI gene expressed in Escherichia coli BL21(DE3) cells harboring pETI23
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