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Literature summary for 1.14.14.9 extracted from

  • Sucharitakul, J.; Chaiyen, P.; Entsch, B.; Ballou, D.P.
    The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis (2005), Biochemistry, 44, 10434-10442.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information kinetics and thermodynamics, determination of redox potentials of FMN reductase component C1-bound FMN in presence or absence of 4-hydroxyphenylacetate, 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
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?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
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-
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Reaction

Reaction Comment Organism Reaction ID
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O kinetics and reaction mechanism Acinetobacter baumannii

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
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?
4-hydroxyphenylacetate + NADH + O2 high substrate specificity, reduction of enzyme reductase component C1 by NADH occurs in two phases, while in the presence of HPA, the reduction of C1 by NADH occurs in a single phase requiring complex formation of C1 and 4-hydroxyphenylacetate prior to binding of NADH, C1 is specifically reduced by the pro-(S)-hydride, the reaction of reduced C1 with oxygen, the reoxidation reaction is also biphasic, consistent with reduced C1 being a mixture of fast and slow reacting species, rate constants for both phases are the same in the absence and presence of HPA, but in the presence of HPA, the equilibrium shifts toward the faster reacting species Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
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?
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 ?
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?

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
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Acinetobacter baumannii
p-hydroxyphenylacetate 3-hydroxylase
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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
FMN a flavoprotein, provides reduced flavin for the oxygenase component of the enzyme to hydroxylate 4-hydroxyphenylacetate, the apoenzyme of the FMN reductase component C1 binds to oxidized FMN tightly in presence of the substrate Acinetobacter baumannii
NADH
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Acinetobacter baumannii