EC Number |
Protein Variants |
Reference |
---|
1.13.12.16 | H152A |
His152 likely functions as the catalytic base that initiates oxidation of neutral substrates by abstracting a proton from the alpha-carbon |
674590 |
1.13.12.16 | H152A |
site-directed mutagenesis. His152 likely functions as the catalytic base that initiates oxidation of neutral substrates by abstracting a proton from the alpha-carbon |
674590 |
1.13.12.16 | H179D |
mutant enzyme shows no activity. Crystal structure of mutant H179D is determined: The structural superimposition of wild-type Sa-NAO and mutant H179D-nitroethane shows no significant structural variation |
724175 |
1.13.12.16 | H179K |
mutant enzyme shows no activity |
724175 |
1.13.12.16 | H179V |
mutant enzyme shows no activity |
724175 |
1.13.12.16 | H196N |
site-directed mutagenesis, does to catalyze the formation of ethylnitronate from nitroethane. It is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate |
685283 |
1.13.12.16 | H196N |
the H196N variant form of the enzyme does to catalyze the formation of ethylnitronate from nitroethane. The H196N variant is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate |
685283 |
1.13.12.16 | H199A |
mutant shows no enzymatic function |
728077 |
1.13.12.16 | more |
construction of an enzyme deletion mutant by the in vivo recombination system of the yeast Saccharomyces cerevisiae strain InvSc1, overview. Quantitative RT-PCR enzyme expression analysis. The expression of ddlA is not changed in the DELTAnmoA mutant compared to the wild-type |
745219 |
1.13.12.16 | S288A |
mutant enzyme forms inclusion bodies when overexpressed in Escherichia coli |
674590 |