KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baumannii | - |
- |
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Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O | kinetics and reaction mechanism | Acinetobacter baumannii |
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 | 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 | Comment | Organism |
---|---|---|
HPAH | - |
Acinetobacter baumannii |
p-hydroxyphenylacetate 3-hydroxylase | - |
Acinetobacter baumannii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Acinetobacter baumannii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Acinetobacter baumannii |
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 | - |
Acinetobacter baumannii |