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Literature summary 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
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.9 | additional information | enzyme is induced by 4-hydroxyphenylacetate, requiring NAD(P)H-flavin oxidoreductase HpaC for delivering of sufficient amounts of FADH2 | Escherichia coli |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.5.1.36 | recombinant overexpression of His-tagged wild-type enzymes HpaC and Fre in strain BL21(DE3), complementation of the inactivation mutant by transient expression of different gene hpaC variants, overview | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.5.1.36 | additional information | construction of an HpaC inactivation mutant strain W-KO | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.36 | HpaB | presence and binding of HpaB reduced the enzyme activity of HpaC due to stabilization and reduced oxidation by O2 of FADH2 | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.36 | additional information | - |
additional information | kinetics, binding studies of HpaC and HpaB | Escherichia coli | |
| 1.5.1.36 | 0.0008 | - |
FAD | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli |  |
| 1.5.1.36 | 0.003 | - |
FAD | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
| 1.5.1.36 | 0.076 | - |
NADH | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
| 1.5.1.36 | 0.183 | - |
NADH | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli | |
| 1.14.14.9 | 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)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.36 | FAD + NAD(P)H | Escherichia coli | - |
FADH2 + NAD(P)+ | - |
? | |
| 1.5.1.36 | additional information | Escherichia coli | the enzyme supplies reduced FADH2 for other enzymes, e.g. the 4-hydroxylphenylacetate 3-monooxygenase HpaB, which contains bound FADH2 and which protects FADH2 from being oxidized by O2, HpaC binds to HpaB without substrate channeling | ? | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + O2 | Escherichia coli | first enzyme in 4-hydroxyphenylacetate metabolism | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 1.14.14.9 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.36 | Escherichia coli | - |
ATCC 11105, genes hpaC and fre encoding the NAD(P)H-flavin oxidoreductase HpaC and the FAD reductase Fre | - |
| 1.14.14.9 | Escherichia coli | - |
ATCC 11105, inducible enzyme HpaB | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.1.36 | recombinant His-tagged wild-type enzymes HpaC and Fre from strain BL21(DE3) | Escherichia coli |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.5.1.36 | additional information | enzyme activities with different growth conditions, overview, strain W-KO does not grow on 4-hydroxyphenylacetate as carbon source | Escherichia coli | - |
| 1.14.14.9 | culture condition:4-hydroxyphenylacetate-grown cell | enzyme induction | Escherichia coli | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.36 | additional information | - |
activity in a coupled assay of HpaB and HpaC | Escherichia coli |
| 1.5.1.36 | 0.318 | - |
strain W-KO, recombinant enzyme Fre, growth on 4-hydroxyphenylacetate as carbon source | Escherichia coli |
| 1.5.1.36 | 25.1 | - |
strain W-KO, recombinant enzyme HpaC, growth on 4-hydroxyphenylacetate as carbon source | Escherichia coli |
| 1.14.14.9 | 0.191 | - |
strain W, induced by 4-hydroxyphenylacetate | Escherichia coli |
| 1.14.14.9 | 3.4 | - |
purified enzyme | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.36 | FAD + NAD(P)H | - |
Escherichia coli | FADH2 + NAD(P)+ | - |
? | |
| 1.5.1.36 | additional information | the enzyme supplies reduced FADH2 for other enzymes, e.g. the 4-hydroxylphenylacetate 3-monooxygenase HpaB, which contains bound FADH2 and which protects FADH2 from being oxidized by O2, HpaC binds to HpaB without substrate channeling | Escherichia coli | ? | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + O2 | - |
Escherichia coli | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + O2 | first enzyme in 4-hydroxyphenylacetate metabolism | Escherichia coli | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 1.14.14.9 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.1.36 | FAD reductase | - |
Escherichia coli |
| 1.5.1.36 | flavin reductase | - |
Escherichia coli |
| 1.5.1.36 | fre | - |
Escherichia coli |
| 1.5.1.36 | HpaC | - |
Escherichia coli |
| 1.5.1.36 | NAD(P)H-flavin oxidoreductase | - |
Escherichia coli |
| 1.14.14.9 | HpaB | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.36 | 30 | - |
assay at, enzyme HpaC | Escherichia coli |
| 1.5.1.36 | 37 | - |
assay at, enzyme Fre | Escherichia coli |
| 1.14.14.9 | 30 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.36 | 40 | - |
NADH | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli | |
| 1.5.1.36 | 40 | - |
FAD | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli | |
| 1.5.1.36 | 178 | - |
NADH | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
| 1.5.1.36 | 178 | - |
FAD | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.36 | 7 | - |
assay at | Escherichia coli |
| 1.14.14.9 | 7 | - |
assay at | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.36 | FADH2 | - |
Escherichia coli | |
| 1.5.1.36 | NADH | - |
Escherichia coli | |
| 1.5.1.36 | NADPH | - |
Escherichia coli | |
| 1.14.14.9 | 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 | |
| 1.14.14.9 | NADH | - |
Escherichia coli | |
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