1.1.1.169	A181L	site-directed mutagenesis, the substitution displaces Ser239 and increases the Km for ketopantoate 844fold, without affecting kcat. The decrease in 2-dehydropantoate affinity enhances the already kinetically preferred NADPH binding path, making the random mechanism appear to be sequentially ordered and reducing the kinetic cooperativity	740065	
1.1.1.169	A181L	the substitution increases the Km of ketopantoate 844fold, without affecting the kcat value	740065	
1.1.1.169	C84A	site-directed mutagenesis	-, 739822	
1.1.1.169	C84A	site-directed mutagenesis, crystal structure analysis, overview	-, 741385	
1.1.1.169	D248A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	667687	
1.1.1.169	D248A	site-directed mutagenesis, wild-type activity	286109	
1.1.1.169	E210A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	667687	
1.1.1.169	E210A	site-directed mutagenesis, wild-type activity	286109	
1.1.1.169	E240A	site-directed mutagenesis, wild-type activity	286109	
1.1.1.169	E256A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	687675	
1.1.1.169	E256A	site-directed mutagenesis, nearly inactive mutant, 2600fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain	667687	
1.1.1.169	E256A	site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme	286109	
1.1.1.169	E256D	wild-type activity	286109	
1.1.1.169	K176A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	687675	
1.1.1.169	K176A	site-directed mutagenesis, nearly inactive mutant, 78000fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain	667687	
1.1.1.169	K176A	site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme	286109	
1.1.1.169	K176A/E256A	double mutant, no activity	286109	
1.1.1.169	K176C	wild-type activity	286109	
1.1.1.169	K72A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	687675	
1.1.1.169	K72A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	667687	
1.1.1.169	K72A	site-directed mutagenesis, wild-type activity	286109	
1.1.1.169	additional information	generation of a gene TK1968 disruption mutant	-, 736827	
1.1.1.169	additional information	Lys176 acts as general acid in ketopantoate reduction and is involved in catalysis and ketopantoate binding, E256A functions in D-pantoate and ketopantoate binding in ketopantoate reductase	286109	
1.1.1.169	additional information	Lys176 and Glu256 important for binding ketopantoate and the catalytic mechanism	286110	
1.1.1.169	N98A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	687675	
1.1.1.169	N98A	site-directed mutagenesis, nearly inactive mutant, 4000fold reduced catalytic efficiency, no complementation of a panE knockout mutant strain	667687	
1.1.1.169	R31A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	687675	
1.1.1.169	S244A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	687675	
1.1.1.169	S244A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	667687	
1.1.1.169	W129A	site-directed mutagenesis	-, 739822	
1.1.1.169	Y60A	site-directed mutagenesis	-, 739822