2.6.1.79	A168G	site-directed mutagenesis, altered substrate binding kinetics compared to wild-type	759965	
2.6.1.79	E108K	site-directed mutagenesis, altered substrate binding kinetics compared to wild-type	759965	
2.6.1.79	K12G	naturally occuring mutant, the incompetent PATs of Rhizobium meliloti (UniProt ID P58350) has a G instead of K12 and shows reduced PAT activity at prephenate concentrations up to 2.5 mM using a coupled assay method. The mutant shows reduced activity and altered kinetics compared to the wild-type	759178	
2.6.1.79	K169S	site-directed mutagenesis, inactive with aspartate and glutamate	759965	
2.6.1.79	K169V	site-directed mutagenesis, inactive with glutamate, altered substrate binding kinetics compared to wild-type	759965	
2.6.1.79	K306A	site-directed mutagenesis, structure comparison with wild-type, overview. The alanine substitution of Lys306 prevents Schiff base formation with the cofactor, inactive mutant	759965	
2.6.1.79	additional information	site-directed mutagenesis, modeling, and molecular dynamics simulations reveal that K/R/Q12 residue (numbering according to Thermus thermophilus 1beta AAT) is a signature of the PAT function of 1beta AAT. It is present in the N-terminal flexible loop only in PAT competent 1beta-AAT and has a possible role in stabilizing prephenate by interacting with its 4-hydroxy group	759178	
2.6.1.79	R445G	site-directed mutagenesis, inactive mutant	759965	
2.6.1.79	T84V	site-directed mutagenesis, altered substrate binding kinetics compared to wild-type	759965	
2.6.1.79	T84V/K169V	site-directed mutagenesis, altered substrate binding kinetics compared to wild-type	759965