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Literature summary extracted from

  • Chaiyen, P.; Suadee, C.; Wilairat, P.
    A novel two-protein component flavoprotein hydroxylase. p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii (2001), Eur. J. Biochem., 268, 5550-5561.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.9 FAD inhibitory effect at more than 0.15 mM Acinetobacter baumannii
1.14.14.9 FMN inhibitory effect at more than 0.15 mM Acinetobacter baumannii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.9 0.012
-
NADH apparent, with FMN Acinetobacter baumannii
1.14.14.9 0.014
-
4-hydroxyphenylacetate apparent, with FAD Acinetobacter baumannii
1.14.14.9 0.019
-
4-hydroxyphenylacetate apparent, with FMN Acinetobacter baumannii
1.14.14.9 0.028
-
NADH apparent, with FAD Acinetobacter baumannii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.9 19000
-
2 * 19000 small component, 2 * 59000 large component Escherichia coli
1.14.14.9 30750
-
2 * 30750, small component Pseudomonas putida
1.14.14.9 32000
-
x * 32000, small component, SDS-PAGE Acinetobacter baumannii
1.14.14.9 38500
-
1 * 38500, large component Pseudomonas putida
1.14.14.9 50000
-
homotetramer, 4 * 50000, large component, SDS-PAGE Acinetobacter baumannii
1.14.14.9 59000
-
2 * 19000 small component, 2 * 59000 large component Escherichia coli
1.14.14.9 73000
-
component C1, gel filtration Acinetobacter baumannii
1.14.14.9 209000
-
component C2, gel filtration Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 Escherichia coli
-
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 Pseudomonas putida
-
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 Acinetobacter baumannii biodegradation of aromatic compounds 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.9 Acinetobacter baumannii
-
-
-
1.14.14.9 Escherichia coli
-
-
-
1.14.14.9 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.9
-
Escherichia coli
1.14.14.9
-
Pseudomonas putida
1.14.14.9 protamine sulfate precipitation, ion-exchange, gel filtration Acinetobacter baumannii

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.9 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O different from other hydroxylases. Two-protein component enzyme: component C1 is a flavoprotein and C2 the hydroxylase component. Mechanism: 4-hydroxyphenylacetate binds to C1, then the enzyme-bound flavin is reduced by NADH, this reduced flavin is transferred to C2 and the reoxidation of the flavin occurs concurrently with the hydroxylation of the substrate 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 8.89
-
C2 component Acinetobacter baumannii
1.14.14.9 201
-
C1 component Acinetobacter baumannii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.9 3-hydroxyphenylacetate + NAD(P)H + O2 98% of 4-hydroxyphenylacetate activity Acinetobacter baumannii 3,4-hydroxyphenylacetate + NAD(P)+ + H2O
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2
-
Escherichia coli 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2
-
Pseudomonas putida 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2
-
Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 biodegradation of aromatic compounds Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 additional information
-
Escherichia coli ?
-
?
1.14.14.9 additional information
-
Pseudomonas putida ?
-
?
1.14.14.9 additional information a variety of aromatic compounds that contain a hydroxyl group in para-position can be hydroxylated. 4-hydroxyphenylacetate hydroxylase is an effector for C1 and substrate for C2 Acinetobacter baumannii ?
-
?
1.14.14.9 phenylacetic acid + ?
-
Pseudomonas putida ?
-
?
1.14.14.9 phenylacetic acid + ? 97% of 4-hydroxyphenylacetate activity Acinetobacter baumannii ?
-
?

Subunits

EC Number Subunits Comment Organism
1.14.14.9 dimer 2 * 30750, small component Pseudomonas putida
1.14.14.9 dimer x * 32000, small component, SDS-PAGE Acinetobacter baumannii
1.14.14.9 dimer 2 * 19000 small component, 2 * 59000 large component Escherichia coli
1.14.14.9 monomer 1 * 38500, large component Pseudomonas putida
1.14.14.9 tetramer homotetramer, 4 * 50000, large component, SDS-PAGE Acinetobacter baumannii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.14.9 25
-
assay at Acinetobacter baumannii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.9 7.5
-
-
Pseudomonas putida
1.14.14.9 7.5
-
assay at Acinetobacter baumannii

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.9 FAD
-
Escherichia coli
1.14.14.9 FAD alternative to FMN for C1 Acinetobacter baumannii
1.14.14.9 FAD tightly associated with small component, native cofactor Pseudomonas putida
1.14.14.9 FADH2
-
Escherichia coli
1.14.14.9 FADH2
-
Acinetobacter baumannii
1.14.14.9 FMN
-
Escherichia coli
1.14.14.9 FMN native cofactor for C1 component Acinetobacter baumannii
1.14.14.9 FMNH2
-
Acinetobacter baumannii
1.14.14.9 NADH
-
Escherichia coli
1.14.14.9 NADH
-
Pseudomonas putida
1.14.14.9 NADH
-
Acinetobacter baumannii
1.14.14.9 NADPH
-
Escherichia coli
1.14.14.9 riboflavin
-
Escherichia coli
1.14.14.9 riboflavin component C1 Acinetobacter baumannii