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Results 1 - 10 of 24 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9D205E activity with D-2-chloropropionate is 10.1% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 13fold higher compared to mutant enzyme 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9D205N catalytically inactive variant 756727
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9D205N no activity with D-2-chloropropionate -, 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9F281A activity with D-2-chloropropionate is 54.7% compared to activity of the wild-type enzyme 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9G50A activity with D-2-chloropropionate is 5.1% compared to activity of the wild-type enzyme -, 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9I52G activity with D-2-chloropropionate is 1.5% compared to activity of the wild-type enzyme 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9L285I activity with D-2-chloropropionate is 24.4% compared to activity of the wild-type enzyme 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9L288A the mutant enzyme is active toward L-enantiomers. The catalytic efficiency is less than 30% of mutant enzyme L288I 756727
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9L288I activity with D-2-chloropropionate is 37.2% compared to activity of the wild-type enzyme 758426
Display the word mapDisplay the reaction diagram Show all sequences 3.8.1.9L288I the mutation enlarges the size of the channel and allows the enzyme to accommodate L-enantiomers (L-2-bromopropionate). The wing flip of I288 induces hydrophobic interactions with the L-enantiomer and directly affects the catalytic efficiency 756727
Results 1 - 10 of 24 > >>