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Results 1 - 10 of 45 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3A151V production by site-directed mutagenesis, alanine ist essential for activity, mutation of residue 151 located at the entryway to the active site reveals that FnGR is very sensitive to increased steric bulk at this position 701927
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3A75T Ki: 0.661 mM (inhibitor: D-glutamate). Turnover number: 1.78/sec (substrate: L-glutamate), 0.065/sec (substrate: D-glutamate). Km: 7.4 mM (substrate: L-glutamate), Km: 0.275 mM (substrate: D-glutamate) 676152
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C184A mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme 2116
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C185A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold 674336
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C185S decrease in racemization activity, mutant retains its gyrase inhibition ability 694039
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C188A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold 674336
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C73A mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme 2116
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C74A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold 674336
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C75S decrease in racemization activity, mutant retains its gyrase inhibition ability 694039
Show all pathways known for 5.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.3C75SC185S less than 10% of wild-type activity, mutant retains its gyrase inhibition ability 694039
Results 1 - 10 of 45 > >>