7.1.1.1	A246C	reverse activity stronger affected than cyclic activity	658003	
7.1.1.1	A253C	reverse activity stronger affected than cyclic activity	658003	
7.1.1.1	A348C	mutation introduced into a cysteine-free mutant enzyme, mutant shows markedly reduced activity	392663	
7.1.1.1	A390C	mutation introduced into a cysteine-free mutant enzyme	392663	
7.1.1.1	A398C	the mutant with wild type activity shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme	733772	
7.1.1.1	A432C	mutation in domain III, reverse reaction in the presence of domain I from R. rubrum, 150% higher reaction rate than wild-type domain III/R. rubrum domain I mixture	392667	
7.1.1.1	A432C	the mutant shows increased ratios between the rates of the forward and reverse reactions, thus approaching that of the wild type enzyme	733772	
7.1.1.1	C292T/C339T/C395S/C397T/C435S	cysteine of the alpha subunits replaced, similar activity as wild-type	392662	
7.1.1.1	C292T/C339T/C395S/C397T/C435S/C147S/C260S	all 7 cysteines of the enzyme, 5 localized in the alpha subunit and 2 in the beta subunit, are replaced, the cysteine-free mutant shows about 5fold more activity in the reduction of acetylpyridine adenine dinucleotide by NADH than wild-type, the cyclic reduction of acetylpyridine adenine dinucleotide by NADH via NADPH is 2-2.5fold more activ	392662	
7.1.1.1	D135N	mutation has no effect in binding affinity of either NAD+ or NADH	674550