Information on EC 1.14.13.135 - 1-hydroxy-2-naphthoate hydroxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.135
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RECOMMENDED NAME
GeneOntology No.
1-hydroxy-2-naphthoate hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-hydroxy-2-naphthoate + NAD(P)H + H+ + O2 = 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
1-hydroxy-2-naphthoate,NAD(P)H:oxygen oxidoreductase (2-hydroxylating, decarboxylating)
The enzyme is involved in the catabolic pathway for the degradation of chrysene in some bacteria [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phenanthrene-degrading
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Manually annotated by BRENDA team
phenanthrene-degrading
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Manually annotated by BRENDA team
no activity in Pseudomonas putida
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Manually annotated by BRENDA team
no activity in Pseudomonas putida CSV86
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-hydroxy-2-naphthoate + NAD(P)H + O2
1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
show the reaction diagram
1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + NAD+ + H2O + CO2
show the reaction diagram
1-hydroxy-2-naphthoate + NADPH + O2
1,2-dihydroxynaphthalene + NADP+ + H2O + CO2
show the reaction diagram
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a flavoprotein monooxygenase specific for 1-hydroxy-2-naphthoic acid, no activity with any other hydroxynaphthoic acid analogues, o-phthalic acid, 3,4-dihydroxybenzoic acid, or salicylic acid
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-hydroxy-2-naphthoate + NAD(P)H + O2
1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
show the reaction diagram
1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + NAD+ + H2O + CO2
show the reaction diagram
1-hydroxy-2-naphthoate + NADPH + O2
1,2-dihydroxynaphthalene + NADP+ + H2O + CO2
show the reaction diagram
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a flavoprotein monooxygenase specific for 1-hydroxy-2-naphthoic acid, no activity with any other hydroxynaphthoic acid analogues, o-phthalic acid, 3,4-dihydroxybenzoic acid, or salicylic acid
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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holoenzyme contains FAD. Km is 0.0047 mM. Preparation of the apoenzyme by the acid-ammonium sulfate, at 2 M, dialysis method, the apoenzyme is colorless, inactive and loses the characteristic flavin absorption spectra but regains about 90% of maximal activity when reconstituted with FAD
NADH
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Vmax/Km is similar for NADPH and NADH
NADPH
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Vmax/Km is similar for NADPH and NADH
additional information
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FMN is a poor substitute for FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no effect by 1 mM of Fe2+, Fe3+, Mg2+, Mn2+, Ca2+, Zn2+, and Cu2+, and by metal chelators, such as EDTA, 2,2-dipyridyl and 1',10'-phenanthroline, at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0716 - 0.0755
1-hydroxy-2-naphthoate
0.087
NADH
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pH 7.5, 30C
0.0846
NADPH
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pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0031
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salicylate-grown cells, pH 7.5, 30C
0.0877
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phenanthrene-grown cells, pH 7.5, 30C
25.3
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purified enzyme, cofactor NADPH, pH 7.5, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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5 min, cell-free extract, the enzyme is stable in presence of 1-hydroxy-2-naphthoic acid
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1-hydroxy-2-naphthoic acid hydroxylase in the cell-free extract is stabilized by 0.1 mM 1-hydroxy-2-naphthoic acid, 5 mM FAD, 2 mM DTT, and 5% glycerol
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repeated freezing and thawing led to inactivation of the enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified enzyme, stabilized by 0.1 mM 1-hydroxy-2-naphthoic acid, 5 mM FAD, 2 mM DTT, and 5% glycerol, retains 100% activity, after 60 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 81fold by heat treatment at 60C, ammonium sulfate fractionation and anion exchange chromatography. Additional purification steps, such as hydrophobic interaction chromatography or gel filtration, lead to the total or a significant, 70%, loss of activity, respectively, without achieving any further purification
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by growth on phenanthrene