1.1.1.B4	A90S	activity with NADPH as cofactor decreased to about 50% of wild-type, activity with NADH strongly decreased	711860	
1.1.1.B4	C295A	the mutant shows an increased size of the alkyl group which can bind in the substrate small pocket by one carbon atom compared to the wild-type enzyme	741784	
1.1.1.B4	G37D/R38P	activity with NADH is decreased relative to Arg38Pro alone, but is higher than that of the wild-type enzyme	711860	
1.1.1.B4	I86A	site-directed mutagensis, the secondary alcohol dehydrogenase I86A mutant is stereospecific for (R)-alcohols instead of (S)-alcohols, in contrast to the wild-type enzyme, the mutation I86A allows large substituents to fit into the large pocket of I86ATeSADH, which corresponds to the small pocket in wild-type TeSADH, modeling of the stereopreference of TeSADH I86A	723841	
1.1.1.B4	I86A	the mutant shows altered substrate specificity and expands substrate specificity to include acetophenone, which is a very poor substrate for wild-type SADH, but also reverses the usual preferred stereochemistry to produce the anti-prelog R-product. I86A SADH exhibits limited reactivity with substituted acetophenones, fluorine being the only tolerable substituent	741784	
1.1.1.B4	I86A/C295A	the mutant enzyme shows broadened substrate specificity for aryl ketones and broadened substrate specificity for meta-substituted, but not para-substituted, acetophenones compared to the wild-type enzyme. The increase of the substrate specificity of I86A/C295A SADH is accompanied by a decrease in the kcat/Km values of acetophenones, possibly due to the substrates fitting loosely inside the more open active site	741784	
1.1.1.B4	M140I	no activity with NADPH as cofactor	711860	
1.1.1.B4	R38P	no activity with NADPH as cofactor, fourfold increase in activity with NADH	711860	
1.1.1.B4	S154Y	mutant exhibits nearly 13fold, 5.4fold, and 2.3fold increase in kcat/Km value, kcat value, and specific activity toward 3,5-bis(trifluoromethyl)acetophenone	-, 739942	
1.1.1.B4	S154Y/L194I	180% of wild-type activity	-, 739942	
1.1.1.B4	V112D	no activity with NADPH as cofactor, strongly decreased activity with NADH	711860	
1.1.1.B4	W95L/N249Y	the mutant exhibits higher activity but decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+ and NADH compared to the wild type enzyme, optimum pH is at about pH 8.6	697839