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Literature summary extracted from
- Purification and characterization of the assimilatory NADPH-nitrate reductase of Aspergillus nidulans (1982), J. Biochem., 91, 761-774.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.3 | FAD | activates 10fold by addition of 0.004 mM, stabilizes against heat inactivation | Aspergillus nidulans |  |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.3 | azide | - |
Aspergillus nidulans | |
| 1.7.1.3 | cyanide | 99% inhibition at 10 mM | Aspergillus nidulans | |
| 1.7.1.3 | p-chloromercuribenzoate | reversion of the inhibition by addition of reduced glutathione | Aspergillus nidulans | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.7.1.3 | 0.045 | - |
NADPH | + nitrate | Aspergillus nidulans | |
| 1.7.1.3 | 0.2 | - |
nitrate | cosubstrate NADPH | Aspergillus nidulans | |
| 1.7.1.3 | 2.5 | - |
FADH2 | + nitrate | Aspergillus nidulans | |
| 1.7.1.3 | 3 | - |
FMNH2 | + nitrate | Aspergillus nidulans | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.3 | Molybdenum | molybdoflavoprotein | Aspergillus nidulans | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.7.1.3 | 38000 | - |
2 * 59000 + 2 * 38000, SDS-PAGE, after heat-treatment all polypeptide chains are 59 kDa | Aspergillus nidulans |
| 1.7.1.3 | 59000 | - |
2 * 59000 + 2 * 38000, SDS-PAGE, after heat-treatment all polypeptide chains are 59 kDa | Aspergillus nidulans |
| 1.7.1.3 | 180000 | - |
gel filtration, sucrose density gradient | Aspergillus nidulans |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.1.3 | nitrate + NADPH | Aspergillus nidulans | - |
nitrite + NADP+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.7.1.3 | Aspergillus nidulans | - |
IFO No. 6083 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.7.1.3 | ammonium slufate precipitation, ion-exchange, gel filtration, hydroxylapatite column. FAD and EDTA essential in all buffers during purification | Aspergillus nidulans |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.7.1.3 | 15.5 | - |
- |
Aspergillus nidulans |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.7.1.3 | -80°C, 0.02 mM FAD, several months with only slight loss of the activity | Aspergillus nidulans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.1.3 | nitrate + NADPH | - |
Aspergillus nidulans | nitrite + NADP+ + H2O | - |
? | |
| 1.7.1.3 | nitrate + NADPH | 4 activities: NADPH-nitrate reductase, FADH-nitrate reductase, reduced methyl viologen-nitrate reductase and NADPH-cytochrome c reductase | Aspergillus nidulans | nitrite + NADP+ + H2O | - |
? | |
| 1.7.1.3 | nitrate + NADPH | catalyzes the NADPH-linked reduction of ferricyanide and 2,6-dichlorophenolindophenol, chlorate- and bromate-dependent NADPH oxidation, and FMNH-linked nitrate reduction | Aspergillus nidulans | nitrite + NADP+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.7.1.3 | tetramer | 2 * 59000 + 2 * 38000, SDS-PAGE, after heat-treatment all polypeptide chains are 59 kDa | Aspergillus nidulans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.7.1.3 | 30 | - |
assay at | Aspergillus nidulans |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.7.1.3 | 37 | - |
absence of FAD, rapid loss of activity, decreases to 50% in less than 20 min | Aspergillus nidulans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.7.1.3 | 7 | 8 | - |
Aspergillus nidulans |
| 1.7.1.3 | 7.4 | - |
assay at | Aspergillus nidulans |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.3 | cytochrome b557 | involved in intracellular electron transport from NADPH to nitrate | Aspergillus nidulans | |
| 1.7.1.3 | FAD | contains 5.91-7.78 nmol FAD per mg of protein, activation of NADPH-nitrate reductase activity | Aspergillus nidulans | |
| 1.7.1.3 | FAD | molybdoflavoprotein | Aspergillus nidulans | |
| 1.7.1.3 | additional information | NADH: no effect, presence of protoheme IX | Aspergillus nidulans |
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