1.20.1.1	additional information	12 x PTDH mutant, saturation mutagenesis performed separately on each of the following residues in the parent PTDH template: V71, E130, Q132, Q137, I150, Q215, R275, L276, I313, V315, A319, and A325. The most thermostabilizing mutation discovered for each particular site is incorporated into the 12 x PTDH mutant, performed for K132, H137, L275, and C276, forming an optimized thermally stable phosphite dehydrogenase termed Opt12. Addition of A146S to Opt12 leads to the Opt13 variant, and the further addition of F198M leads to Opt14	691424	
1.20.1.1	H292F	almost complete loss of activity	658120	
1.20.1.1	H292K	almost complete loss of activity	658120	
1.20.1.1	H292N	almost complete loss of activity	-, 658120	
1.20.1.1	R237H	almost complete loss of activity	658120	
1.20.1.1	R237L	almost complete loss of activity	658120	
1.20.1.1	R237Q	almost complete loss of activity	658120	
1.20.1.1	E175A/A176R	double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor	-, 657956, 658259	
1.20.1.1	D79N	has kinetic parameters more similar to those of wild-type	690884	
1.20.1.1	E266Q	higher activity, steady-state and pre-steady-state rates are comparable	-, 690884