EC Number   |
Protein Variants |
Reference |
|---|
   1.5.1.42 | more |
design of a stable immobilizing reagent for bioluminescent analysis using luciferase, EC 1.14.14., from a recombinant Escherichia coli strain and NADH:FMN-oxidoreductase, EC 1.5.1.42. Natural polymers, gelatin and starch, are used to create a viscous, structured microenvironment for the NADH:FMN-oxidoreductase-luciferase system. Evaluation of the stability of the coupled enzyme system, overview. Both gelatin and starch have a stabilizing effect on the enzymes, the enzymes' activity is increased 2fold in the presence of 1% and 5% of gelatin at 20°C and 25°C, respectively. The acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol/l) is observed, thermal inactivation rate constants of the enzymes at 25-43°C are unchanged |
741589 |
| 1.5.1.42 | more |
establishment of a coupled pure enzyme bioluminescent system and usage for NADH detection |
-, 765526 |
| 1.5.1.42 | more |
replacement of the wild-type spectator residue of the rate-limiting step of the reduction of FMN to FMNH2 catalysed by DszD and known to play an important role in the reaction energy profile. As replacements, all the naturally occurring amino acids are used, one at a time, using computational methodologies, determination of mutant activities, application of quantum mechanics/molecular mechanics (QM/MM) methods within an ONIOM scheme |
764492 |
| 1.5.1.42 | more |
the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate |
-, 743144 |
| 1.5.1.42 | N33A |
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type |
764492 |
| 1.5.1.42 | N33C |
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type |
764492 |
| 1.5.1.42 | N33D |
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type |
764492 |
| 1.5.1.42 | N33E |
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type |
764492 |
| 1.5.1.42 | N33F |
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type |
764492 |
| 1.5.1.42 | N33G |
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type |
764492 |
