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Results 1 - 10 of 13 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10A77T/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
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10L104A 1.5-fold increase in kcat and a decrease in KM values for 3'-methyl-alpha-phenylalanine and styryl-alpha-alanine substrates 721637
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10L108E site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme 747670
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10L108E/N458F site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme 747670
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10L97G 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
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10L97G/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
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10L97G/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
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10more 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
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10N231A site-directed mutagenesis, a cofactor MIO-less, catalytically inactive mutant 747670
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10N458F site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme 747670
Results 1 - 10 of 13 > >>