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Results 1 - 10 of 57 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5A165F decreased degree of amide formation compared to the wild type enzyme and forms about 3% phenylglycine amide from (R,S)-phenylglycinonitrile. In contrast to the wild-type enzyme, the variant almost exclusively forms (R)-phenylglycine. This point mutation results in an almost complete stereoinversion of the reaction -, 755880
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5A114F inactive 710940
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5G109F inactive 710940
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5Y54I inactive -, 718648
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5Y54K inactive -, 718648
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5Y54R inactive 718648
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5R128K mutant demonstrates low enantioselectivity (44.9% enantiomeric excess) as compared with the wild-type enzyme (52.7% enantiomeric excess) -, 755936
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5R128E mutant displays no activity toward mandelonitrile 755936
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5A136Y/I168Y mutant enzyme produces (R)-mandelic acid with an enantiomeric excess value of 89.7%, an R-enantioselectivity higher than that obtained with the single mutations A136Y and I168Y 755936
Display the word mapDisplay the reaction diagram Show all sequences 3.5.5.5A136Y mutant enzyme shows reversed selectivity and preferentially produces (R)-mandelic acid with an enantiomeric excess values of 66.7% -, 755936
Results 1 - 10 of 57 > >>