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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.135
-
RECOMMENDED NAME
GeneOntology No.
1-hydroxy-2-naphthoate hydroxylase
-
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
-
-
-
-
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
-
-
Manually annotated by BRENDA team
phenanthrene-degrading
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas putida
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas putida CSV86
-
-
-
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
-
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
-
-
?
additional information
?
-
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
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
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
-
Vmax/Km is similar for NADPH and NADH
NADPH
-
Vmax/Km is similar for NADPH and NADH
additional information
-
FMN is a poor substitute for FAD
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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
-
pH 7.5, 30°C
0.0846
NADPH
-
pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0031
-
salicylate-grown cells, pH 7.5, 30°C
0.0877
-
phenanthrene-grown cells, pH 7.5, 30°C
25.3
-
purified enzyme, cofactor NADPH, pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
-
2 * 34000, SDS-PAGE
66000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
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
-
repeated freezing and thawing led to inactivation of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 81fold by heat treatment at 60°C, 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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by growth on phenanthrene