EC Number |
Protein Variants |
Reference |
---|
1.5.1.40 | G29L |
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme |
763787 |
1.5.1.40 | G29S |
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme |
763787 |
1.5.1.40 | G29Y |
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme |
763787 |
1.5.1.40 | I135A |
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme |
741811 |
1.5.1.40 | I135G |
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme |
741811 |
1.5.1.40 | I135V |
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme |
741811 |
1.5.1.40 | more |
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 |
1.5.1.40 | more |
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 |
1.5.1.40 | P89H |
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme |
763787 |
1.5.1.40 | P89L |
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme |
763787 |