Any feedback?
Literature summary extracted from
- Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration (2005), FEBS J., 272, 3816-3827.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 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 | Stutzerimonas stutzeri |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.20.1.1 | E175A/A176R | mutant utilizes both NAD+ and NADP+, kinetic isotope effects study, hydride transfer step is partially rate determining | Stutzerimonas stutzeri |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.20.1.1 | Stutzerimonas stutzeri | - |
- |
- |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
