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Literature summary for 1.14.14.9 extracted from

  • Thotsaporn, K.; Sucharitakul, J.; Wongratana, J.; Suadee, C.; Chaiyen, P.
    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.
    View publication on PubMed
Search for more literature for 1.14.14.9

Cloned(Commentary)

Cloned (Comment) Organism
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
15
-
 4-hydroxyphenylacetate native C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate Acinetobacter baumannii
16
-
 4-hydroxyphenylacetate recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate Acinetobacter baumannii
21
-
 NADH native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate Acinetobacter baumannii
22
-
 NADH native and recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate Acinetobacter baumannii
25
-
 4-hydroxyphenylacetate native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate Acinetobacter baumannii
26
-
 4-hydroxyphenylacetate recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate Acinetobacter baumannii
28
-
 NADH recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate Acinetobacter baumannii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE Acinetobacter baumannii
47000
-
 x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii Q6Q271 gene c1-hpah; enzyme is a two-protein component hydroxylase, consisting of components C1 and C2 both required for activity
-
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)

Purification (Comment) Organism
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.3
-
 purified recombinant C2 component Acinetobacter baumannii
200
-
 purified recombinant C1 component Acinetobacter baumannii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2
-
 Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?

Subunits

Subunits Comment Organism
? x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE Acinetobacter baumannii
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

Synonyms Comment Organism
HPAH
-
 Acinetobacter baumannii
More enzyme belongs to the two-protein component class of aromatic hydroxylases Acinetobacter baumannii
p-hydroxyphenylacetate 3-hydroxylase
-
 Acinetobacter baumannii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
343
-
 4-hydroxyphenylacetate native C1-C2 system or complete enzyme, respectively, pH 7.5 Acinetobacter baumannii
389
-
 4-hydroxyphenylacetate recombinant C1-C2 system or complete enzyme, respectively, pH 7.5 Acinetobacter baumannii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
FAD FMN and FAD can substitute for each other, required Acinetobacter baumannii
FMN FMN and FAD can substitute for each other, required Acinetobacter baumannii
NADH required Acinetobacter baumannii