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Literature summary for 1.14.14.9 extracted from
- Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase (2003), Biochemistry, 42, 7509-7517.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme is induced by 4-hydroxyphenylacetate, requiring NAD(P)H-flavin oxidoreductase HpaC for delivering of sufficient amounts of FADH2 | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, FADH2/FAD binding capacity, enzyme kinetics in a coupled assay with HpaC, a NAD(P)H-flavin oxidoreductase | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxyphenylacetate + NADH + O2 | Escherichia coli | first enzyme in 4-hydroxyphenylacetate metabolism | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? |  |
| additional information | Escherichia coli | the enzyme does not form stable complexes or channel substrates with the NAD(P)H-flavin oxidoredctase HpaC, but NAD(P)H-flavin oxidoreductase HpaC is required for delivering of sufficient amounts of FADH2 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
ATCC 11105, inducible enzyme HpaB | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture condition:4-hydroxyphenylacetate-grown cell | enzyme induction | Escherichia coli | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.191 | - |
strain W, induced by 4-hydroxyphenylacetate | Escherichia coli |
| 3.4 | - |
purified enzyme | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxyphenylacetate + NADH + O2 | - |
Escherichia coli | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 4-hydroxyphenylacetate + NADH + O2 | first enzyme in 4-hydroxyphenylacetate metabolism | Escherichia coli | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| additional information | the enzyme does not form stable complexes or channel substrates with the NAD(P)H-flavin oxidoredctase HpaC, but NAD(P)H-flavin oxidoreductase HpaC is required for delivering of sufficient amounts of FADH2 | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HpaB | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FADH2 | bound to the enzyme in vivo, which has a high affinity for FADH2, cosubstrate needs to be protected by the enzyme against oxidation to FAD by O2 | Escherichia coli | |
| NADH | - |
Escherichia coli | |
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