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Results 1 - 10 of 29 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40G29L site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme 763787
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40G29S site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme 763787
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40G29Y site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme 763787
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40I135A site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40I135G site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40I135V site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40more engineering of the thermostable F420:NADPH oxidoreductase from Thermobifida fusca (Tfu-FNO) by structure-inspired site-directed mutagenesis to accommodate the unnatural N1 substituents of eight nicotinamide cofactor biomimetics (NCBs). The extraordinarily low redox potential of the natural cofactor F420H2 is then exploited to reduce these NCBs. Wild-type enzyme has detectable activity toward all selected NCBs. Saturation mutagenesis at positions Gly29 and Pro89 results in mutants with up to 139times higher catalytic efficiencies, kinetics comparisons, overview. Most mutations significantly decrease the activity toward NADP+ but do not completely inhibit the enzyme for this cosubstrate 763787
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40more pre-steady-state data with F420 cofactor and NADPH for the enzyme Fno mutant variants reveal biphasic kinetics with a fast and slow phase, similar with wild-type Fno, overview 741811
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40P89H site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme 763787
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.40P89L site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme 763787
Results 1 - 10 of 29 > >>