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Literature summary for 1.14.14.9 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
Search for more literature for 1.14.14.9

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information transient kinetic study, overview Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2 Acinetobacter baumannii high substrate specificity 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Subunits Comment Organism
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

Synonyms Comment Organism
HPAH
-
 Acinetobacter baumannii
p-hydroxyphenylacetate 3-hydroxylase
-
 Acinetobacter baumannii

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
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
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
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
NADH
-
 Acinetobacter baumannii