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Literature summary extracted from
- Alkyne substrate interaction within the nitrogenase MoFe protein (2007), J. Inorg. Biochem., 101, 1642-1648.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.18.6.1 | 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 |
| 1.18.6.1 | 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 |
| 1.18.6.1 | 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 |
| 1.18.6.1 | 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 |
| 1.18.6.1 | V70I | site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene | Azotobacter vinelandii |
| 1.19.6.1 | 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 |
| 1.19.6.1 | 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 |
| 1.19.6.1 | 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 |
| 1.19.6.1 | 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 |
| 1.19.6.1 | V70I | site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene | Azotobacter vinelandii |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.18.6.1 | Fe2+ | in [Fe-S] clusters | Azotobacter vinelandii |  |
| 1.18.6.1 | Mg2+ | - |
Azotobacter vinelandii | |
| 1.19.6.1 | Fe2+ | in [Fe-S] clusters | Azotobacter vinelandii | |
| 1.19.6.1 | 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 | 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 | ? | - |
? | |
| 1.18.6.1 | 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 | ? | - |
? | |
| 1.19.6.1 | 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 | ? | - |
? | |
| 1.19.6.1 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.18.6.1 | Azotobacter vinelandii | - |
- |
- |
| 1.18.6.1 | Azotobacter vinelandii DJ995 | - |
- |
- |
| 1.19.6.1 | Azotobacter vinelandii | - |
- |
- |
| 1.19.6.1 | Azotobacter vinelandii DJ995 | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.18.6.1 | 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 | ? | - |
? | |
| 1.18.6.1 | 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 | ? | - |
? | |
| 1.18.6.1 | 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 | ? | - |
? | |
| 1.18.6.1 | 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 | ? | - |
? | |
| 1.19.6.1 | 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 | ? | - |
? | |
| 1.19.6.1 | 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 | ? | - |
? | |
| 1.19.6.1 | 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 | ? | - |
? | |
| 1.19.6.1 | 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
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.18.6.1 | ATP | - |
Azotobacter vinelandii | |
| 1.18.6.1 | FeMo cofactor | structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein | Azotobacter vinelandii | |
| 1.18.6.1 | 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 | |
| 1.19.6.1 | ATP | - |
Azotobacter vinelandii | |
| 1.19.6.1 | FeMo cofactor | structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein | Azotobacter vinelandii | |
| 1.19.6.1 | 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 |
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