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

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EC NUMBER
COMMENTARY hide
1.14.13.33
-
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RECOMMENDED NAME
GeneOntology No.
4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
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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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
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-
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
95471-33-3
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PB4
-
-
Manually annotated by BRENDA team
strain PB4
-
-
Manually annotated by BRENDA team
no activity in Ralstonia paucula
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-
-
Manually annotated by BRENDA team
strain JJ-1b
-
-
Manually annotated by BRENDA team
strain JJ-1b
-
-
Manually annotated by BRENDA team
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
flavoprotein, 0.8 FAD per enzyme molecule
NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for full activity in low concentrations of phosphate buffer, most effective at 5 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dihydroxybenzoate
-
over 70% inhibition at 10 mM
2,5-Dihydroxybenzoate
-
over 70% inhibition at 10 mM
2-Hydroxybenzoate
-
over 70% inhibition at 10 mM
3-hydroxybenzoate
-
-
4-Aminobenzoate
-
over 70% inhibition at 10 mM
4-Fluorobenzoate
-
-
Cl-
-
non-competitive
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
4-hydroxybenzoate
-
-
0.045
NADH
-
pH 7.0-8.4
0.063 - 0.17
NADPH
-
Km increases as pH rises from 7.0 to 8.4
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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
-
crude cell extract
0.36
-
for 4-hydroxybenzoate in the presence of NADPH
0.47
-
for 4-hydroxybenzoate in the presence of NADH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.8
-
pH 6.2: about 50% of activity maximum, pH 8.8: about 70% of activity maximum, NADPH
6.5 - 8.8
-
50% of activity maximum at pH 6.5 and pH 8.8, NADH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
x * 41000, SDS-PAGE
47000
-
PAGE of native and denatured enzyme
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 47000, PAGE of native and denatured enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 8.5
-
4°C, 24 h, stable
438880
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
rapid inactivation above, p-hydroxybenzoate protects against heat inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
praI gene expressed in Escherichia coli BL21(DE3) cells harboring pETI23
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.33)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)