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	additional information	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