EC Number   |
Application |
Reference |
|---|
    2.7.1.26 | drug development |
HsRFK parameters differ from those of the so far evaluated bacterial counterparts, suggesting species-specific mechanisms in RFK catalysis. Thus, HsRFK is a potential therapeutic target because of its key functions, while bacterial RFK modules are potential antimicrobial targets |
759167 |
| 2.7.1.26 | synthesis |
immobilized enzyme is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile method for preparing exclusively other synthetic methods, the 5'-phosphates |
641244 |
| 2.7.1.26 | synthesis |
the enzyme is used for the preparation of flavin mononucleotide (FMN) and FMN analogues from their corresponding riboflavin precursors, which is performed in a two-step procedure. After initial enzymatic conversion of riboflavin to FAD by the bifunctional FAD synthetase, the adenyl moiety of FAD is hydrolyzed with snake venom phosphodiesterase to yield FMN. The engineered FAD synthetase from Corynebacterium ammoniagenes with deleted N-terminal adenylation domain is a biocatalyst that is stable and efficient for direct and quantitative phosphorylation of riboflavin and riboflavin analogues to their corresponding FMN cofactors at preparative-scale |
739570 |
