5.4.3.10	A77T/I79S/C89T/L97G	site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme with reduced beta-ladder and 3_10-helix contents	746591	
5.4.3.10	L104A	1.5-fold increase in kcat and a decrease in KM values for 3'-methyl-alpha-phenylalanine and styryl-alpha-alanine substrates	721637	
5.4.3.10	L108E	site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme	747670	
5.4.3.10	L108E/N458F	site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme	747670	
5.4.3.10	L97G	site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme, the mutant has a significant increase in 310-helix and beta-ladder, compared to wild-type, with the highest coil percent among the PAM variants and improved activity. The mutant shows reduced temperature stability and optimum for PAM activity, in contrast to PAL activity	746591	
5.4.3.10	L97G/A77T/C89T	site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme with reduced beta-ladder and 3_10-helix contents	746591	
5.4.3.10	L97G/C89T	site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme, the mutant has a significant increase in 310-helix and beta-ladder compared to wild-type. The mutant shows reduced temperature stability and optimum for PAM activity, in contrast to PAL activity	746591	
5.4.3.10	additional information	mutation of the inner loop region, that closes the active site of PAM, within PAM (PAM residues 77-97) in a stepwise approach. Almost all of the single loop mutations trigger a lyase phenotype in PAM. Experimental and computational evidence suggest that the induced lyase features result from inner loop mobility enhancements, which are possibly caused by a 310-helix cluster, flanking alpha-helices, and hydrophobic interactions. The application of wild-type PAM for the synthesis of beta-amino acids is hindered by low reaction rates and the mixture of alpha-Phe and beta-Phe generated from the asymmetric synthetic route. Molecular dynamic simulations	746591	
5.4.3.10	N231A	site-directed mutagenesis, a cofactor MIO-less, catalytically inactive mutant	747670	
5.4.3.10	N458F	site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme	747670	
5.4.3.10	N458L	site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme	747670	
5.4.3.10	Y322A	site-directed mutagenesis, a cofactor MIO-less, catalytically inactive mutant	747670	
5.4.3.10	Y80A	site-directed mutagenesis	747670