EC Number   |
Protein Variants |
Reference |
|---|
    1.19.6.1 | alphaH195Q |
site-directed mutagenesis, the mutant shows an altered electron transfer substrate specificity compared to the wild-type enzyme,overview |
686108 |
| 1.19.6.1 | alphaQ191K |
site-directed mutagenesis, the mutant shows reduced electron transfer activity compared to the wild-type enzyme, it reduces only H+, not N2, overview |
686108 |
| 1.19.6.1 | more |
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 |
-, 688191 |
| 1.19.6.1 | more |
construction of Qalpha191K, Halpha195Q, nifValpha, Qalpha191K/nifValpha and Halpha195Q/nifValpha mutants and determination of their substrate specificity, the mutant strains all show reduced electron transfer, overview |
686108 |
| 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 |
-, 688191 |
| 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 |
-, 688191 |
| 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 |
-, 688191 |
| 1.19.6.1 | V70I |
site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene |
-, 688191 |
