EC Number |
Protein Variants |
Reference |
---|
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 | more |
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 |