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	additional information	has great potential for cofactor regeneration	-, 690884	
1.20.1.1	additional information	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