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Literature summary for 1.14.14.9 extracted from

  • Ruangchan, N.; Tongsook, C.; Sucharitakul, J.; Chaiyen, P.
    pH-Dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase (2011), J. Biol. Chem., 286, 223-233.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.9

Inhibitors

Inhibitors Comment Organism Structure
4-hydroxyphenylacetate inhibition of the dehydration step by 4-hydroxyphenylacetate at pH 9.0 Acinetobacter baumannii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information reaction kinetics of C2-FMNH with oxygen at various pH values investigated by stopped-flow and rapid quenched-flow techniques, detailed overview Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylacetate + NADH + H+ + O2 Acinetobacter baumannii via C2-FMNH-, and C4a-hydroperoxy-FMN and C4a-hydroxy-FMN 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
additional information Acinetobacter baumannii the enzyme is a flavin-dependent two-component monooxygenase that consists of a reductase component and an oxygenase component C2. C2 catalyzes the hydroxylation of HPA using oxygen and reduced FMN as co-substrates. All flavin-dependent monooxygenases perform oxygenation through the participation of a reactive intermediate, C4a-hydroperoxy-flavin ?
-
 ?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
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-
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Acinetobacter baumannii Q6Q272
-
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + NADH + H+ + O2 via C2-FMNH-, and C4a-hydroperoxy-FMN and C4a-hydroxy-FMN Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
additional information the enzyme is a flavin-dependent two-component monooxygenase that consists of a reductase component and an oxygenase component C2. C2 catalyzes the hydroxylation of HPA using oxygen and reduced FMN as co-substrates. All flavin-dependent monooxygenases perform oxygenation through the participation of a reactive intermediate, C4a-hydroperoxy-flavin Acinetobacter baumannii ?
-
 ?
additional information decreased accumulation of the intermediate at higher pH is due to the greater rates of C4a-hydroxy-FMN decay caused by the abolishment of substrate inhibition in the dehydration step at high pH Acinetobacter baumannii ?
-
 ?
additional information in the absence of 4-hydroxyphenylacetate, the rate constant for the formation of C4a-hydroperoxy-FMN is unaffected at pH 6.2-9.9. The rate constant for the following H2O2 elimination step increases with higher pH, consistent with a pKa above 9.4. In the presence of 4-hydroxyphenylacetate, the rate constants for the formation of C4a-hydroperoxy-FMN and the ensuing hydroxylation step are not significantly affected by the pH. In contrast, the following steps of C4a-hydroxy-FMN dehydration to form oxidized FMN occur through two pathways that are dependent on the pH of the reaction. One pathway, dominant at low pH, allows the detection of a C4a-hydroxy-FMN intermediate, whereas the pathway dominant at high pH produces oxidized FMN without an apparent accumulation of the intermediate. Both pathways efficiently catalyze hydroxylation without generating significant amounts of wasteful H2O2 at pH 6.2-9.9 Acinetobacter baumannii ?
-
 ?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 in the absence of 4-hydroxyphenylacetate, the rate constant for the formation of C4a-hydroperoxy-FMN is unaffected at pH 6.2-9.9. The rate constant for the following H2O2 elimination step increases with higher pH, consistent with a pKa above 9.4. In the presence of 4-hydroxyphenylacetate, the rate constants for the formation of C4a-hydroperoxy-FMN and the ensuing hydroxylation step are not significantly affected by the pH. In contrast, the following steps of C4a-hydroxy-FMN dehydration to form oxidized FMN occur through two pathways that are dependent on the pH of the reaction. One pathway, dominant at low pH, allows the detection of a C4a-hydroxy-FMN intermediate, whereas the pathway dominant at high pH produces oxidized FMN without an apparent accumulation of the intermediate. Both pathways efficiently catalyze hydroxylation without generating significant amounts of wasteful H2O2 at pH 6.2-9.9 Acinetobacter baumannii
7
-
 assay at Acinetobacter baumannii

pH Range

pH Minimum pH Maximum Comment Organism
6.2 9.9 assay range for determination of reaction kinetics of C2-FMNH with oxygen at various pH values investigated by stopped-flow and rapid quenched-flow techniques, detailed overview Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
FMN dependent on Acinetobacter baumannii
NADH
-
 Acinetobacter baumannii