Application | Comment | Organism |
---|---|---|
biotechnology | (±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate | Thermoplasma acidophilum |
synthesis | (±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate | Thermoplasma acidophilum |
Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli, short-chain dehydrogenase/reductase from Thermus thermophilus HB8 and the glucose dehydrogenase from Thermoplasma acidophilum DSM 1728 are simultaneously over-expressed by heterologous expression with pETDuet | Thermoplasma acidophilum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40250 | - |
calculated from sequence | Thermoplasma acidophilum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoplasma acidophilum | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
NAD(P)-dependent glucose dehydrogenase | - |
Thermoplasma acidophilum |