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Literature summary for 1.20.1.1 extracted from

  • Woodyer, R.; Zhao, H.; van der Donk, W.A.
    Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration (2005), FEBS J., 272, 3816-3827.
    View publication on PubMed

Application

Application Comment Organism
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 Pseudomonas stutzeri

Protein Variants

Protein Variants Comment Organism
E175A/A176R mutant utilizes both NAD+ and NADP+, kinetic isotope effects study, hydride transfer step is partially rate determining Pseudomonas stutzeri

Organism

Organism UniProt Comment Textmining
Pseudomonas stutzeri
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