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Literature summary for 1.18.6.1 extracted from

  • Barney, B.M.; Igarashi, R.Y.; Dos Santos, P.C.; Dean, D.R.; Seefeldt, L.C.
    Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis (2004), J. Biol. Chem., 279, 53621-53624.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
V70A site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme Azotobacter vinelandii
V70I site-directed mutagenesis, decreased the hydrazine reduction activity Azotobacter vinelandii
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

Inhibitors

Inhibitors Comment Organism Structure
N2 inhibits hydrazine reduction Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km for N2 of wild-type and mutant enzyme Azotobacter vinelandii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced ferredoxin + H+ + N2 + ATP + H2O Azotobacter vinelandii
-
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
ir

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.13
-
V70I mutant, substrate acetylene, in presence of C2H4 Azotobacter vinelandii
0.17
-
V70I mutant, substrate N2, in presence of NH3 Azotobacter vinelandii
0.2
-
wild-type enzyme, substrate acetylene, in presence of H2 Azotobacter vinelandii
0.6
-
wild-type enzyme, substrate N2, in presence of NH3 Azotobacter vinelandii
0.64
-
wild-type enzyme, substrate N2, in presence of H2 Azotobacter vinelandii
1.8
-
wild-type enzyme, substrate acetylene, in presence of C2H4 Azotobacter vinelandii
1.94
-
V70I mutant, substrate N2, in presence of H2 Azotobacter vinelandii
2
-
V70I mutant, substrate acetylene, in presence of H2 Azotobacter vinelandii
2.02
-
wild-type enzyme, substrate argon, in presence of H2 Azotobacter vinelandii
2.34
-
V70I mutant, substrate argon, in presence of H2 Azotobacter vinelandii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylene + ?
-
Azotobacter vinelandii ethylene + ?
-
?
hydrazine + ? high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme Azotobacter vinelandii ?
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
-
Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
ir

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Azotobacter vinelandii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8 assay at, hydrazine reduction activity Azotobacter vinelandii
7
-
assay at, N2 reduction activity Azotobacter vinelandii

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Azotobacter vinelandii
iron-molybdenum cofactor substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis Azotobacter vinelandii