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Results 1 - 9 of 9
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16F156H/G157L site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16F156L/G157F site-directed mutagenesis, the mutations improve the hydrophobic active site pocket increasing enzyme selectivity and stereospecificity 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16F156N/G157Y site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme -, 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16F450C site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme -, 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16F450I site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme -, 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16G119S/F450Y site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme -, 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16more active site mutations to improve enantioselectivity of the enzyme towards 4-substituted cyclohexanone substrates, method evaluation, overview, the effect of mutation of residues 449 and 450 does not have a full impact on the improvement of the hydrophobic pocket -, 677179
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16more completion of the formal total synthesis of (+)-showdomycin and establishing of the absolute configuration of biooxidation product as (1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one, overview 673035
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.16more mutations in the active site residues responsible for stereoselectivity is a shortcut to an improvement in enantioselectivity in the often unselective CPMO, the combination of rational design and random mutagenesis at the predefined positions gives rise to focused libraries for improvement of the catalytic performance of enzymes, including enhanced enantioselectivity, using Complete Active Site Saturation Test, CAST, overview -, 675582
Results 1 - 9 of 9