Any feedback?
Literature summary for 1.5.1.36 extracted from
- Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase (2003), Biochemistry, 42, 7509-7517.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of an HpaC inactivation mutant strain W-KO | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, binding studies of HpaC and HpaB | Escherichia coli | |
| 0.0008 | - |
FAD | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli |  |
| 0.003 | - |
FAD | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
| 0.076 | - |
NADH | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
| 0.183 | - |
NADH | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FAD + NAD(P)H | Escherichia coli | - |
FADH2 + NAD(P)+ | - |
? | |
| 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 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
ATCC 11105, genes hpaC and fre encoding the NAD(P)H-flavin oxidoreductase HpaC and the FAD reductase Fre | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type enzymes HpaC and Fre from strain BL21(DE3) | Escherichia coli |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | enzyme activities with different growth conditions, overview, strain W-KO does not grow on 4-hydroxyphenylacetate as carbon source | Escherichia coli | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
activity in a coupled assay of HpaB and HpaC | Escherichia coli |
| 0.318 | - |
strain W-KO, recombinant enzyme Fre, growth on 4-hydroxyphenylacetate as carbon source | Escherichia coli |
| 25.1 | - |
strain W-KO, recombinant enzyme HpaC, growth on 4-hydroxyphenylacetate as carbon source | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FAD + NAD(P)H | - |
Escherichia coli | FADH2 + NAD(P)+ | - |
? | |
| 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 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FAD reductase | - |
Escherichia coli |
| flavin reductase | - |
Escherichia coli |
| fre | - |
Escherichia coli |
| HpaC | - |
Escherichia coli |
| NAD(P)H-flavin oxidoreductase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at, enzyme HpaC | Escherichia coli |
| 37 | - |
assay at, enzyme Fre | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 40 | - |
NADH | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli | |
| 40 | - |
FAD | recombinant enzyme Fre, pH 7.0, 37°C | Escherichia coli | |
| 178 | - |
NADH | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
| 178 | - |
FAD | recombinant enzyme HpaC, pH 7.0, 30°C | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FADH2 | - |
Escherichia coli | |
| NADH | - |
Escherichia coli | |
| NADPH | - |
Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
