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Literature summary extracted from
- Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases (2004), Biochim. Biophys. Acta, 1680, 60-66.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.9 | genes c1-hpah and c2-hpah, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3), the recombinant enzyme is similarly active cmpared to the native one | Acinetobacter baumannii |
| 1.14.14.9 | genes c1-hpah and c2-hpah, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3), the recombinant enzyme is similarly active compared to the native one | Acinetobacter baumannii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.9 | 15 | - |
4-hydroxyphenylacetate | native C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate | Acinetobacter baumannii |  |
| 1.14.14.9 | 16 | - |
4-hydroxyphenylacetate | recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate | Acinetobacter baumannii | |
| 1.14.14.9 | 21 | - |
NADH | native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate | Acinetobacter baumannii | |
| 1.14.14.9 | 22 | - |
NADH | native and recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate | Acinetobacter baumannii | |
| 1.14.14.9 | 25 | - |
4-hydroxyphenylacetate | native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate | Acinetobacter baumannii | |
| 1.14.14.9 | 26 | - |
4-hydroxyphenylacetate | recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate | Acinetobacter baumannii | |
| 1.14.14.9 | 28 | - |
NADH | recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate | Acinetobacter baumannii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.9 | 35000 | - |
x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE | Acinetobacter baumannii |
| 1.14.14.9 | 47000 | - |
x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE | Acinetobacter baumannii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.9 | Acinetobacter baumannii | Q6Q271 | gene c1-hpah; enzyme is a two-protein component hydroxylase, consisting of components C1 and C2 both required for activity | - |
| 1.14.14.9 | Acinetobacter baumannii | Q6Q272 | gene c2-hpah; enzyme is a two-protein component hydroxylase, consisting of components C1 and C2 both required for activity | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.9 | recombinant enzyme components C1 and C2 from Escherichia coli strain BL21(DE3), C1 4.0fold, C2 1.81fold | Acinetobacter baumannii |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.9 | 8.3 | - |
purified recombinant C2 component | Acinetobacter baumannii |
| 1.14.14.9 | 200 | - |
purified recombinant C1 component | Acinetobacter baumannii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + O2 | - |
Acinetobacter baumannii | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.14.9 | ? | x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE | Acinetobacter baumannii |
| 1.14.14.9 | More | enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation | Acinetobacter baumannii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.9 | HPAH | - |
Acinetobacter baumannii |
| 1.14.14.9 | More | enzyme belongs to the two-protein component class of aromatic hydroxylases | Acinetobacter baumannii |
| 1.14.14.9 | p-hydroxyphenylacetate 3-hydroxylase | - |
Acinetobacter baumannii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.9 | 343 | - |
4-hydroxyphenylacetate | native C1-C2 system or complete enzyme, respectively, pH 7.5 | Acinetobacter baumannii | |
| 1.14.14.9 | 389 | - |
4-hydroxyphenylacetate | recombinant C1-C2 system or complete enzyme, respectively, pH 7.5 | Acinetobacter baumannii | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.9 | 7.5 | - |
assay at | Acinetobacter baumannii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.9 | FAD | FMN and FAD can substitute for each other, required | Acinetobacter baumannii | |
| 1.14.14.9 | FMN | FMN and FAD can substitute for each other, required | Acinetobacter baumannii | |
| 1.14.14.9 | NADH | required | Acinetobacter baumannii | |
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