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Literature summary for 1.14.13.33 extracted from

  • Fujii, T.; Kaneda, T.
    Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum (1985), Eur. J. Biochem., 147, 97-104.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2,4-Dihydroxybenzoate over 70% inhibition at 10 mM Corynebacterium cyclohexanicum
2,5-Dihydroxybenzoate over 70% inhibition at 10 mM Corynebacterium cyclohexanicum
2-Hydroxybenzoate over 70% inhibition at 10 mM Corynebacterium cyclohexanicum
3-hydroxybenzoate
-
Corynebacterium cyclohexanicum
4-Aminobenzoate over 70% inhibition at 10 mM Corynebacterium cyclohexanicum
4-Fluorobenzoate
-
Corynebacterium cyclohexanicum
Cl- non-competitive Corynebacterium cyclohexanicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.035
-
4-hydroxybenzoate
-
Corynebacterium cyclohexanicum
0.045
-
NADH pH 7.0-8.4 Corynebacterium cyclohexanicum
0.063 0.17 NADPH Km increases as pH rises from 7.0 to 8.4 Corynebacterium cyclohexanicum

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Corynebacterium cyclohexanicum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for full activity in low concentrations of phosphate buffer, most effective at 5 mM Corynebacterium cyclohexanicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
PAGE of native and denatured enzyme Corynebacterium cyclohexanicum

Organism

Organism UniProt Comment Textmining
Corynebacterium cyclohexanicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Corynebacterium cyclohexanicum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
30.5
-
NADPH Corynebacterium cyclohexanicum

Storage Stability

Storage Stability Organism
-20°C, several months Corynebacterium cyclohexanicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxybenzoate + NAD(P)H + O2 enzyme is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at approximately equal rates Corynebacterium cyclohexanicum 3,4-dihydroxybenzoate + NAD(P)+ + H2O
-
?
4-hydroxybenzoate + NADH + H+ + O2
-
Corynebacterium cyclohexanicum 3,4-dihydroxybenzoate + NAD+ + H2O
-
r

Subunits

Subunits Comment Organism
monomer 1 * 47000, PAGE of native and denatured enzyme Corynebacterium cyclohexanicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Corynebacterium cyclohexanicum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
10 min, stable Corynebacterium cyclohexanicum
65
-
rapid inactivation above, p-hydroxybenzoate protects against heat inactivation Corynebacterium cyclohexanicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
NADPH Corynebacterium cyclohexanicum
7.8
-
NADH Corynebacterium cyclohexanicum

pH Range

pH Minimum pH Maximum Comment Organism
6.2 8.8 pH 6.2: about 50% of activity maximum, pH 8.8: about 70% of activity maximum, NADPH Corynebacterium cyclohexanicum
6.5 8.8 50% of activity maximum at pH 6.5 and pH 8.8, NADH Corynebacterium cyclohexanicum

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.3 8.5 4°C, 24 h, stable Corynebacterium cyclohexanicum

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein, 0.8 FAD per enzyme molecule Corynebacterium cyclohexanicum
NADH
-
Corynebacterium cyclohexanicum
NADPH
-
Corynebacterium cyclohexanicum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.029 0.045 Cl-
-
Corynebacterium cyclohexanicum