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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.6.1 N2 inhibits hydrazine reduction Azotobacter vinelandii

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Mg2+
-
 Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
-
-
-

Reaction

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
a

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.6.1 30
-
 assay at Azotobacter vinelandii

pH Optimum

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

Cofactor

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