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Results 1 - 10 of 99 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47G113S enhanced thermal stability compared to wild-type enzyme, mutant enzyme retains slight higher activity than the wild-type enzyme in an acidic environment, so the mutant enzyme maybe more effective for synthesis of (S)-cyanohydrin than the wild-type enzyme 650692
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128A substitution of tryptophan128 by an alanine residue enlarges the entrance channel to the active site of MeHNL and thus facilitates access of sterically demanding substrates to the active site, increased conversion rate towards 3-phenoxybenzaldehyde, octan-3-one and heptan-3-one 650854
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128C mutation increases the specific activity towards 4-hydroxymandelonitrile of the various MeHNL mutant compared to the wild-type enzyme 650854
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128L mutation increases the specific activity towards 4-hydroxymandelonitrile of the various MeHNL mutant compared to the wild-type enzyme 650854
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128Y mutation increases the specific activity towards 4-hydroxymandelonitrile of the various MeHNL mutant compared to the wild-type enzyme 650854
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47C81A specific activity is 93% of the wild-type value 653781
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47T11A specific activity is 24fold lower than that of the wild-type enzyme 653781
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128A activity with the natural substrate 2-hydroxy-2-methylpropanenitrile (acetone cyanohydrin) is 70% of wild-type activity. The specific activities of MeHNL-W128A for the unnatural substrates mandelonitrile and 4-hydroxymandelonitrile are increased 9fold and 450fold, respectively, compared with the wild-type. The crystal structure of the mutant W128A substrate free form at 2.1 A resolution indicates that the W128A substitution has significantly enlarged the active-site channel entrance, and thereby explains the observed changes in substrate specificity for bulky substrates 653798
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128A mutant enzyme is (S)-selective as the wild-type enzyme 661490
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.47W128C mutant enzyme is (S)-selective as the wild-type enzyme 661490
Results 1 - 10 of 99 > >>