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Literature summary extracted from

  • Sucharitakul, J.; Chaiyen, P.; Entsch, B.; Ballou, D.P.
    Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii (2006), J. Biol. Chem., 281, 17044-17053.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.9 additional information
-
 additional information transient kinetic study, overview 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 Acinetobacter baumannii high substrate specificity 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.9 Acinetobacter baumannii
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.9 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O kinetic reaction mechanisms of the smaller FMN reductase enzyme component C1 and the larger oxygenase enzyme component C2, C2 shows a random order kinetic mechanism, detailed overview Acinetobacter baumannii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 high substrate specificity Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 hydroxylation occurs from the ternary complex forming the C2-C(4a)-hydroxy-FMN-3,4-dihydroxyphenylacetate complex Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
1.14.14.9 additional information the enzyme is a two-protein system consisting of a smaller FMN reductase component C1 and a larger oxygenase component C2, C1 exists as a mixture of isoforms Acinetobacter baumannii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.9 More the enzyme is a two-protein system consisting of a smaller FMN reductase component C1 and a larger oxygenase component C2, C1 exists as a mixture of isoforms Acinetobacter baumannii

Synonyms

EC Number Synonyms Comment Organism
1.14.14.9 HPAH
-
 Acinetobacter baumannii
1.14.14.9 p-hydroxyphenylacetate 3-hydroxylase
-
 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
-
 assay at Acinetobacter baumannii

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.9 FAD a flavoprotein, provides reduced flavin FAD- for the enzyme oxygenase component C2 to hydroxylate 4-hydroxyphenylacetate, the complex of C2-FADH2 reacts with oxygen to form C(4a)-hydroperoxy-FAD, the C2-FADH2-4-hydroxyphenylacetate complex reacts more slowly Acinetobacter baumannii
1.14.14.9 FMN a flavoprotein, provides reduced flavin FMNH- for the enzyme oxygenase component C2 to hydroxylate 4-hydroxyphenylacetate, the complex of C2-FMNH2 reacts with oxygen to form C(4a)-hydroperoxy-FMN, the C2-FMNH2-4-hydroxyphenylacetate complex reacts more slowly Acinetobacter baumannii
1.14.14.9 additional information hydroxyphenylacetate forms a dead end complex with the (C2-C4a)-hydroxy-FMN intermediate inhibiting the bound flavin from returning to the oxidized form, FADH2 is equally active, the enzyme oxygenase component C2 has the unusual ability to use both common flavin cofactors in catalysis, kinetics, overview Acinetobacter baumannii
1.14.14.9 NADH
-
 Acinetobacter baumannii