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Results 1 - 5 of 5
EC Number Protein Variants Commentary Reference
Show all pathways known for 4.1.2.55Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.55T157C improved for 2-dehydro-3-deoxy-D-gluconate with a 75% diastereoisomeric ratio 715259
Show all pathways known for 4.1.2.55Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.55T157C/Y132V diastereoselective formation of 2-dehydro-3-deoxy-D-gluconate with much improved (91%) diastereoisomeric ratio 715259
Show all pathways known for 4.1.2.55Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.55T157F/Y132V diastereoselective formation of 2-dehydro-3-deoxy-D-gluconate with much improved (93%) diastereoisomeric ratio 715259
Show all pathways known for 4.1.2.55Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.55T157V/A198L/D181Q diastereoselective formation of 2-dehydro-3-deoxy-D-galactonate with much improved (88%) diastereoisomeric ratio 715259
Show all pathways known for 4.1.2.55Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.55V193A the mutant enzyme displays a threefold increase in activity compared with wild type enzyme. Increased specific activity at 40–60 °C of this mutant is observed, not only for the condensation of pyruvate with glyceraldehyde, but also for several unnatural acceptor aldehydes. The optimal temperature for activity of SacKdgAV193A is lower than for the wild type enzyme, but enzymatic stability of the mutant is similar to that of the wild type 718713
Results 1 - 5 of 5