EC Number   |
Application |
Reference |
|---|
    1.17.1.9 | analysis |
enzyme may be used for direct spectrophotometric assay of formate |
-, 288090 |
| 1.17.1.9 | biofuel production |
NAD+-dependent formate dehydrogenase is capable of the electrochemical reduction of carbon dioxide into formate, which can be ultimately converted to methanol. Enzyme secretion of formate dehydrogenase by yeast is a promising method for creating multi-enzyme devices for biofuel production |
743726 |
| 1.17.1.9 | biofuel production |
potential applications in NAD(H)-dependent industrial biocatalysis as well as in the production of renewable fuels and chemicals from carbon dioxide. Formate dehydrogenase from Myceliophthora thermophile possess a huge potential for CO2 reduction or NADH generation and under extreme alkaline conditions |
-, 746279 |
| 1.17.1.9 | biotechnology |
FDH from Candida boidinii is an important biocatalyst for the regeneration of the cofactor NADH in industrial enzyme-catalyzed reductions |
711549 |
| 1.17.1.9 | biotechnology |
immobilization of enzyme on highly activated glyoxyl agarose, optimization protocol. Optimized enzyme retains 50% of the offered activity and becomes 50times more stable at high temperature and neutral pH. Optimal temperature increases by 10°C at pH 4.5. Immobilized enzyme accepts dextran-NAD+ as a substrate, use on ultra-filtration reactors to catalyze the recycling of NAD+ |
672513 |
| 1.17.1.9 | biotechnology |
overexpression of the NAD+-dependent formate dehydrogenase in Escherichia coli doubles maximum yield of NADH from 2 to 4 mol NADH/mol glucose consumed |
656695 |
| 1.17.1.9 | biotechnology |
study on stability of recombinant enzyme in homogeneous aequeous solution, at gas-liquid interfaces in a bubble column, and under shear stress. Level of enzyme stability in solution also depends on the enzyme variant employed. Mutants C23S and C23S/C262A perform much better than wild-type in quiescent solution and reactors with little mechanical stress. Mutant C23S/C262A is less stable than wild-type at high stress levels in the Couette viscometer or the bubble column |
672762 |
| 1.17.1.9 | biotechnology |
use of enzyme for regeneration of NADH. Coexpression of alpha-haloketone resistant enzyme mutants and a carbonyl reductase from Kluyveromyces aestuarii for production of ethyl-(S)-4-chloro-3-hydroxybutanoate with optical purity of product of 99% enantiomeric excess, from ethyl-4-chloroacetoacetate |
671509 |
| 1.17.1.9 | drug development |
construction of bifunctional formate dehydrogenase and leucine dehydrogenase enzymatic complex for efficient cofactor regeneration and L-tert leucine biotransformation. L-tert leucine is a widely used chiral building block in many asymmetric reactions for the synthesis of anti-tumor and anti-HIV drugs |
742376 |
| 1.17.1.9 | medicine |
enzyme-loaded erythrocytes along with equimolar solution of sodium carbonate and hydrogencarbonate facilitate removal of formate in methanol poisoning of folate-deficient rats |
673133 |
