Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.18.6.1 extracted from

  • Dos Santos, P.C.; Mayer, S.M.; Barney, B.M.; Seefeldt, L.C.; Dean, D.R.
    Alkyne substrate interaction within the nitrogenase MoFe protein (2007), J. Inorg. Biochem., 101, 1642-1648.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information construction of mutant Azotobacter vinelandii strains DJ1242, DJ1313, and DJ1495, the mutant show loss of the ability to grow under nitrogen fixing conditions, phenotypes, overview Azotobacter vinelandii
Q191A/V70A site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene Azotobacter vinelandii
V70A site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne Azotobacter vinelandii
V70G site-directed mutagenesis, the mutant MoFe protein variant shows an increased capacity for reduction of the terminal alkyne, 1-butyne, but no detectable reduction of the internal alkyne 2-butyne Azotobacter vinelandii
V70I site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene Azotobacter vinelandii

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in [Fe-S] clusters Azotobacter vinelandii
Mg2+
-
Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Azotobacter vinelandii nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth ?
-
?
additional information Azotobacter vinelandii DJ995 nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth ?
-
?

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-
Azotobacter vinelandii DJ995
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth Azotobacter vinelandii ?
-
?
additional information substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview Azotobacter vinelandii ?
-
?
additional information nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth Azotobacter vinelandii DJ995 ?
-
?
additional information substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview Azotobacter vinelandii DJ995 ?
-
?

Cofactor

Cofactor Comment Organism Structure
ATP
-
Azotobacter vinelandii
FeMo cofactor structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein Azotobacter vinelandii
FeMo protein a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein, Fe6 within FeMo-cofactor provides the unique site for alkyne substrate binding and has van der Waals contact with the side chains of alpha-Val70l and alpha-Gln191, overview Azotobacter vinelandii