EC Number |
Application |
Reference |
---|
1.20.1.1 | biotechnology |
application of mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R for regeneration of NADPH in xylose reductase-catalyzed xylitol synthesis and alcohol dehydrogenase-catalyzed (R)-phenylethanol synthesis. comparison of enzyme with commercial Pseudomonas sp. formate dehydrogenase. Mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R shows higher substrate conversion and higher total turnover numbers for NADP+ than formate dehydrogenase |
672712 |
1.20.1.1 | biotechnology |
evaluation of enzyme mutants for regeneration of reduced cofactors NADH and NADPH in industrial processes and comparison with Candida boidinii formate dehydrogenase |
671425 |
1.20.1.1 | biotechnology |
improvement of enzyme for use in regeneration of NADH and NADPH, application in bioconversion of trimethylpyruvate to L-tert-leucine as model reaction |
673144 |
1.20.1.1 | biotechnology |
use of enzyme mutant E175A/A176R for regeneration of NADH and NADPH. Model system converting xylose into xylitol by NADP-dependent xylose reductase and comparison of regeneration of NADPH by enzyme mutant and by Pseudomonas sp. formate dehydrogenase |
673526 |
1.20.1.1 | more |
has great potential for cofactor regeneration |
-, 690884 |
1.20.1.1 | more |
random mutagenesis followed by comprehensive saturation mutagenesis further improves the enzyme thermostability while maintaining its activity. Mutant has improved the half-life of thermal inactivation at 45°C by 23,000fold over the parent enzyme. The engineered phosphite dehydrogenase will be useful in NAD(P)H regeneration |
691424 |
1.20.1.1 | synthesis |
production of deuterium- or tritium-labeled substances, mutant enzymes could be applied as NADPH regeneration systems |
-, 657956, 658259 |