EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.18.6.1 | V70A | site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme | Azotobacter vinelandii |
1.18.6.1 | V70I | site-directed mutagenesis, decreased the hydrazine reduction activity | Azotobacter vinelandii |
1.18.6.1 | V70X | site-directed mutagenesis, substitution of valine with an amino acid with a smaller side chain increases the hydrazine reduction activity, substitution with an amino acid with a larger side chain decreases the enzyme activity with N2, acetylene or hydrazine | Azotobacter vinelandii |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.18.6.1 | N2 | inhibits hydrazine reduction | Azotobacter vinelandii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.6.1 | additional information | - |
additional information | Km for N2 of wild-type and mutant enzyme | Azotobacter vinelandii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.18.6.1 | Mg2+ | - |
Azotobacter vinelandii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.6.1 | reduced ferredoxin + H+ + N2 + ATP + H2O | Azotobacter vinelandii | - |
oxidized ferredoxin + H2 + NH3 + ADP + phosphate | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.6.1 | Azotobacter vinelandii | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.18.6.1 | 4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | active site location | Azotobacter vinelandii |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.18.6.1 | 0.13 | - |
V70I mutant, substrate acetylene, in presence of C2H4 | Azotobacter vinelandii |
1.18.6.1 | 0.17 | - |
V70I mutant, substrate N2, in presence of NH3 | Azotobacter vinelandii |
1.18.6.1 | 0.2 | - |
wild-type enzyme, substrate acetylene, in presence of H2 | Azotobacter vinelandii |
1.18.6.1 | 0.6 | - |
wild-type enzyme, substrate N2, in presence of NH3 | Azotobacter vinelandii |
1.18.6.1 | 0.64 | - |
wild-type enzyme, substrate N2, in presence of H2 | Azotobacter vinelandii |
1.18.6.1 | 1.8 | - |
wild-type enzyme, substrate acetylene, in presence of C2H4 | Azotobacter vinelandii |
1.18.6.1 | 1.94 | - |
V70I mutant, substrate N2, in presence of H2 | Azotobacter vinelandii |
1.18.6.1 | 2 | - |
V70I mutant, substrate acetylene, in presence of H2 | Azotobacter vinelandii |
1.18.6.1 | 2.02 | - |
wild-type enzyme, substrate argon, in presence of H2 | Azotobacter vinelandii |
1.18.6.1 | 2.34 | - |
V70I mutant, substrate argon, in presence of H2 | Azotobacter vinelandii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.6.1 | acetylene + ? | - |
Azotobacter vinelandii | ethylene + ? | - |
? | |
1.18.6.1 | hydrazine + ? | high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme | Azotobacter vinelandii | ? | - |
? | |
1.18.6.1 | reduced ferredoxin + H+ + N2 + ATP + H2O | - |
Azotobacter vinelandii | oxidized ferredoxin + H2 + NH3 + ADP + phosphate | - |
ir |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.18.6.1 | 30 | - |
assay at | Azotobacter vinelandii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.18.6.1 | 7 | 8 | assay at, hydrazine reduction activity | Azotobacter vinelandii |
1.18.6.1 | 7 | - |
assay at, N2 reduction activity | Azotobacter vinelandii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.18.6.1 | Ferredoxin | - |
Azotobacter vinelandii | |
1.18.6.1 | iron-molybdenum cofactor | substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis | Azotobacter vinelandii |