| Autor: |
Bychek IA; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia., Zenchenko AA; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia., Kostromina MA; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia., Khisamov MM; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia., Solyev PN; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia., Esipov RS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia., Mikhailov SN; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia., Varizhuk IV; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia. |
| Abstrakt: |
The enzymatic synthesis of nucleoside derivatives is an important alternative to multi-step chemical methods traditionally used for this purpose. Despite several undeniable advantages of the enzymatic approach, there are a number of factors limiting its application, such as the limited substrate specificity of enzymes, the need to work at fairly low concentrations, and the physicochemical properties of substrates-for example, low solubility. This research conducted by our group is dedicated to the advantages and limitations of using purine nucleoside phosphorylases (PNPs), the main enzymes for the metabolic reutilization of purines, in the synthesis of modified nucleoside analogues. In our work, the substrate specificity of PNP from various bacterial sources (mesophilic and thermophilic) was studied, and the effect of substrate, increased temperature, and the presence of organic solvents on the conversion rate was investigated. |
