Article
In silico protein engineering shows that novel mutations affecting NAD+ binding sites may improve phosphite dehydrogenase stability and activity.
Scientific reports - 1 Feb 2023
Baammi Soukayna, Daoud Rachid, El Allali Achraf
Abstract excerpt
Pseudomonas stutzeri phosphite dehydrogenase (PTDH) catalyzes the oxidation of phosphite to phosphate in the presence of NAD, resulting in the formation of NADH. The regeneration of NADH by PTDH is greater than any other enzyme due to the substantial change in the free energy of reaction (G°' = - 63.3 kJ/mol). Presently, improving the stability of PTDH is for a great importance to ensure an economically viable...
Topics
- NAD
- Molecular Docking Simulation
- Phosphites
- Protein Engineering
- Binding Sites
- Mutation
- Kinetics