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Information on EC 1.14.13.135 - 1-hydroxy-2-naphthoate hydroxylase
for references in articles please use BRENDA:EC1.14.13.135
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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
1.14.13.135 1-hydroxy-2-naphthoate hydroxylase
IUBMB Comments
The enzyme is involved in the catabolic pathway for the degradation of chrysene in some bacteria .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
1-hydroxy-2-naphthoic acid hydroxylase, 1-hydroxy-2-naphthoate hydroxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-hydroxy-2-naphthoate + NAD(P)H + H+ + O2 = 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
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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].
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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
1-hydroxy-2-naphthoate + NADPH + O2
1,2-dihydroxynaphthalene + NADP+ + H2O + CO2
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Substrates: 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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Substrates: substrate specificity, overview. No activity on salicylic acid, 3-hydroxy-2-naphthoic acid, 2-hydroxy-1-naphthoic acid, 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, 3,4-dihydroxybenzoic acid, 1-naphthol, 2-naphthol, 1-naphthoic acid, 2-naphthoic acid, gentisic acid or catechol
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1-hydroxy-2-naphthoate + NAD(P)H + O2
1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
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Substrates: the enzyme is involved in the catabolic pathway for the degradation of chrysene. The proposed catabolic pathway for chrysene degradation by strain PNK-04 is chrysene/hydroxyphenanthroic acid/1-hydroxy-2-naphthoic acid/1,2-dihydroxynaphthalene/salicylic acid/catechol/cis,cis-muconic acid
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Products: -
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1-hydroxy-2-naphthoate + NAD(P)H + O2
1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
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Substrates: the enzyme is involved in the catabolic pathway for the degradation of chrysene. The proposed catabolic pathway for chrysene degradation by strain PNK-04 is chrysene/hydroxyphenanthroic acid/1-hydroxy-2-naphthoic acid/1,2-dihydroxynaphthalene/salicylic acid/catechol/cis,cis-muconic acid
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1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + NAD+ + H2O + CO2
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Substrates: 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
Products: -
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1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + NAD+ + H2O + CO2
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Substrates: 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. In the naphthalene route, 1-hydroxy-2-naphthoic acid is metabolized via 1,2-dihydroxynaphthalene and salicylic acid to catechol by a series of enzymatic steps similar to naphthalene metabolic pathway
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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
1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + NAD+ + H2O + CO2
-
Substrates: 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. In the naphthalene route, 1-hydroxy-2-naphthoic acid is metabolized via 1,2-dihydroxynaphthalene and salicylic acid to catechol by a series of enzymatic steps similar to naphthalene metabolic pathway
Products: -
Products: -
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1-hydroxy-2-naphthoate + NADPH + O2
1,2-dihydroxynaphthalene + NADP+ + H2O + CO2
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Substrates: 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
Products: -
Products: -
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1-hydroxy-2-naphthoate + NAD(P)H + O2
1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
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Substrates: the enzyme is involved in the catabolic pathway for the degradation of chrysene. The proposed catabolic pathway for chrysene degradation by strain PNK-04 is chrysene/hydroxyphenanthroic acid/1-hydroxy-2-naphthoic acid/1,2-dihydroxynaphthalene/salicylic acid/catechol/cis,cis-muconic acid
Products: -
Products: -
?
1-hydroxy-2-naphthoate + NAD(P)H + O2
1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
-
Substrates: the enzyme is involved in the catabolic pathway for the degradation of chrysene. The proposed catabolic pathway for chrysene degradation by strain PNK-04 is chrysene/hydroxyphenanthroic acid/1-hydroxy-2-naphthoic acid/1,2-dihydroxynaphthalene/salicylic acid/catechol/cis,cis-muconic acid
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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significantly lower activity compared to phenanthrene-grown cells
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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in the naphthalene route, 1-hydroxy-2-naphthoic acid is metabolized via 1,2-dihydroxynaphthalene and salicylic acid to catechol by a series of enzymatic steps similar to naphthalene metabolic pathway
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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5 min, cell-free extract, the enzyme is stable in presence of 1-hydroxy-2-naphthoic acid
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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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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
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deveryshetty, J.; Phale, P.S.
Biodegradation of phenanthrene by Alcaligenes sp. strain PPH: partial purification and characterization of 1-hydroxy-2-naphthoic acid hydroxylase
FEMS Microbiol. Lett.
311
93-101
2010
Alcaligenes sp., no activity in Pseudomonas putida, no activity in Pseudomonas putida CSV86
brenda
Nayak, A.S.; Sanjeev Kumar, S.; Santosh, Kumar, M.; Anjaneya, O.; Karegoudar, T.B.
A catabolic pathway for the degradation of chrysene by Pseudoxanthomonas sp. PNK-04
FEMS Microbiol. Lett.
320
128-134
2011
Pseudoxanthomonas sp., Pseudoxanthomonas sp. PNK-04
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.135)
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Release 2023.1 (January 2023)
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