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Literature summary extracted from
- Identification and characterization of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus (1999), J. Biol. Chem., 274, 36715-36721.
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.16.1.10 | 0.061 | - |
NADH | pH 7.0, 85°C | Archaeoglobus fulgidus |  |
| 1.16.1.10 | 0.066 | - |
Fe(III)-EDTA | pH 7.0, 85°C, cosubstrate: NADPH | Archaeoglobus fulgidus | |
| 1.16.1.10 | 0.08 | - |
NADPH | pH 7.0, 85°C | Archaeoglobus fulgidus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.16.1.10 | additional information | high cellular abundance, 0.75% of the total soluble protein | Archaeoglobus fulgidus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.16.1.10 | additional information | the enzyme does not require Mg2+ for optimal activity | Archaeoglobus fulgidus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.10 | 18000 | - |
2 * 18000, SDS-PAGE | Archaeoglobus fulgidus |
| 1.16.1.10 | 18659 | - |
2 * 18659, calculated from sequence | Archaeoglobus fulgidus |
| 1.16.1.10 | 40000 | - |
gel filtration | Archaeoglobus fulgidus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.16.1.10 | Archaeoglobus fulgidus | O29428 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.16.1.10 | - |
Archaeoglobus fulgidus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.10 | 3503 | - |
pH 7.0, 85°C | Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.16.1.10 | 2 Fe(III)-EDTA + NADH | no activity is obtained with uncomplexed Fe3+, i.e. FeCl3 and Fe(OH)3, with the menaquinone analog dimethylnaphthoquinone or with Fe2+-EDTA. The enzyme does not reduce EDTA-chelated Ag+ and Cu2+. With Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor | Archaeoglobus fulgidus | 2 Fe(II)-EDTA + NAD+ + H+ | - |
? | |
| 1.16.1.10 | 2 Fe(III)-EDTA + NADPH | no activity is obtained with uncomplexed Fe3+, i.e. FeCl3 and Fe(OH)3, with the menaquinone analog dimethylnaphthoquinone or with Fe2+-EDTA. The enzyme does not reduce EDTA-chelated Ag+ and Cu2+. With Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor | Archaeoglobus fulgidus | 2 Fe(II)-EDTA + NADP+ + H+ | - |
? | |
| 1.16.1.10 | additional information | the ferric reductase also functions as an NAD(P)H:flavin oxidoreductase | Archaeoglobus fulgidus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.16.1.10 | homodimer | 2 * 18000, SDS-PAGE | Archaeoglobus fulgidus |
| 1.16.1.10 | homodimer | 2 * 18659, calculated from sequence | Archaeoglobus fulgidus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.16.1.10 | AF0830 | - |
Archaeoglobus fulgidus |
| 1.16.1.10 | ferric reductase | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.10 | 85 | - |
assay at | Archaeoglobus fulgidus |
| 1.16.1.10 | 88 | - |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.10 | 50 | 100 | 50°C: about 50% of maximal activity, 100°C: about 50% of maximal activity | Archaeoglobus fulgidus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.10 | 7 | - |
- |
Archaeoglobus fulgidus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.10 | 6 | 8 | pH 6.0: about 40% of maximal activity, pH 8.0: about 60% of maximal activity | Archaeoglobus fulgidus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.16.1.10 | FMN | flavoprotein, enzyme bound flavin is involved in catalysis, contains 1.4 FMN per monomer, non-covalently bound to the enzyme | Archaeoglobus fulgidus | |
| 1.16.1.10 | NADH | with Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor | Archaeoglobus fulgidus | |
| 1.16.1.10 | NADPH | with Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor | Archaeoglobus fulgidus | |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.16.1.10 | Archaeoglobus fulgidus | calculated from sequence | - |
5.84 |
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