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Literature summary extracted from
- Biodegradation of phenanthrene by Alcaligenes sp. strain PPH: partial purification and characterization of 1-hydroxy-2-naphthoic acid hydroxylase (2010), FEMS Microbiol. Lett., 311, 93-101.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.14.13.135 | 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 | Alcaligenes sp. |
| 1.14.13.135 | repeated freezing and thawing led to inactivation of the enzyme | Alcaligenes sp. |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.135 | 0.0716 | - |
1-hydroxy-2-naphthoate | pH 7.5, 30°C, with NADH | Alcaligenes sp. |  |
| 1.14.13.135 | 0.0755 | - |
1-hydroxy-2-naphthoate | pH 7.5, 30°C, with NADPH | Alcaligenes sp. | |
| 1.14.13.135 | 0.0846 | - |
NADPH | pH 7.5, 30°C | Alcaligenes sp. | |
| 1.14.13.135 | 0.087 | - |
NADH | pH 7.5, 30°C | Alcaligenes sp. | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.135 | 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 | Alcaligenes sp. |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.135 | 34000 | - |
2 * 34000, SDS-PAGE | Alcaligenes sp. |
| 1.14.13.135 | 66000 | - |
gel filtration | Alcaligenes sp. |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.1 | salicylate + O2 + NADH + 2 H+ | Alcaligenes sp. | - |
catechol + CO2 + H2O + NAD+ | - |
? | |
| 1.14.13.1 | salicylate + O2 + NADPH + 2 H+ | Alcaligenes sp. | - |
catechol + CO2 + H2O + NADP+ | - |
? | |
| 1.14.13.135 | 1-hydroxy-2-naphthoate + NADH + O2 | Alcaligenes sp. | 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 | 1,2-dihydroxynaphthalene + NAD+ + H2O + CO2 | - |
? | |
| 1.14.13.135 | 1-hydroxy-2-naphthoate + NADPH + O2 | Alcaligenes sp. | 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 | 1,2-dihydroxynaphthalene + NADP+ + H2O + CO2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.1 | Alcaligenes sp. | - |
phenanthrene-degrading | - |
| 1.14.13.135 | Alcaligenes sp. | - |
phenanthrene-degrading | - |
| 1.14.13.135 | no activity in Pseudomonas putida | - |
- |
- |
| 1.14.13.135 | no activity in Pseudomonas putida CSV86 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.13.135 | 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 | Alcaligenes sp. |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.13.1 | culture condition:phenanthrene-grown cell | - |
Alcaligenes sp. | - |
| 1.14.13.1 | culture condition:salicylate-grown cell | - |
Alcaligenes sp. | - |
| 1.14.13.135 | culture condition:phenanthrene-grown cell | - |
Alcaligenes sp. | - |
| 1.14.13.135 | culture condition:salicylate-grown cell | significantly lower activity compared to phenanthrene-grown cells | Alcaligenes sp. | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.1 | 0.0017 | - |
salicylate-grown cells, pH 7.5, 30°C | Alcaligenes sp. |
| 1.14.13.1 | 0.0127 | - |
phenanthrene-grown cells, pH 7.5, 30°C | Alcaligenes sp. |
| 1.14.13.135 | 0.0031 | - |
salicylate-grown cells, pH 7.5, 30°C | Alcaligenes sp. |
| 1.14.13.135 | 0.0877 | - |
phenanthrene-grown cells, pH 7.5, 30°C | Alcaligenes sp. |
| 1.14.13.135 | 25.3 | - |
purified enzyme, cofactor NADPH, pH 7.5, 30°C | Alcaligenes sp. |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.14.13.135 | -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 | Alcaligenes sp. |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.1 | salicylate + O2 + NADH + 2 H+ | - |
Alcaligenes sp. | catechol + CO2 + H2O + NAD+ | - |
? | |
| 1.14.13.1 | salicylate + O2 + NADPH + 2 H+ | - |
Alcaligenes sp. | catechol + CO2 + H2O + NADP+ | - |
? | |
| 1.14.13.135 | 1-hydroxy-2-naphthoate + NADH + O2 | 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 | Alcaligenes sp. | 1,2-dihydroxynaphthalene + NAD+ + H2O + CO2 | - |
? | |
| 1.14.13.135 | 1-hydroxy-2-naphthoate + NADH + O2 | 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 | Alcaligenes sp. | 1,2-dihydroxynaphthalene + NAD+ + H2O + CO2 | - |
? | |
| 1.14.13.135 | 1-hydroxy-2-naphthoate + NADPH + O2 | 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 | Alcaligenes sp. | 1,2-dihydroxynaphthalene + NADP+ + H2O + CO2 | - |
? | |
| 1.14.13.135 | additional information | 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 | Alcaligenes sp. | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.13.135 | homodimer | 2 * 34000, SDS-PAGE | Alcaligenes sp. |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.1 | salicylate hydroxylase | - |
Alcaligenes sp. |
| 1.14.13.1 | salicylate-1-hydroxylase | - |
Alcaligenes sp. |
| 1.14.13.135 | 1-hydroxy-2-naphthoic acid hydroxylase | - |
Alcaligenes sp. |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.1 | 30 | - |
assay at | Alcaligenes sp. |
| 1.14.13.135 | 30 | - |
assay at | Alcaligenes sp. |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.1 | 60 | - |
5 min, cell-free extract, in presence of 1-hydroxy-2-naphthoic acid, inactivation | Alcaligenes sp. |
| 1.14.13.135 | 60 | - |
5 min, cell-free extract, the enzyme is stable in presence of 1-hydroxy-2-naphthoic acid | Alcaligenes sp. |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.1 | 7.5 | - |
assay at | Alcaligenes sp. |
| 1.14.13.135 | 7.5 | - |
- |
Alcaligenes sp. |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.1 | FAD | - |
Alcaligenes sp. | |
| 1.14.13.1 | NADH | - |
Alcaligenes sp. | |
| 1.14.13.1 | NADPH | - |
Alcaligenes sp. | |
| 1.14.13.135 | 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 | Alcaligenes sp. | |
| 1.14.13.135 | additional information | FMN is a poor substitute for FAD | Alcaligenes sp. | |
| 1.14.13.135 | NADH | Vmax/Km is similar for NADPH and NADH | Alcaligenes sp. | |
| 1.14.13.135 | NADPH | Vmax/Km is similar for NADPH and NADH | Alcaligenes sp. | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.14.13.135 | Alcaligenes sp. | the enzyme is induced by growth on phenanthrene | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.13.135 | metabolism | 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 | Alcaligenes sp. |
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