Bacterial Purine Nucleoside Phosphorylases from Mesophilic and Thermophilic Sources: Characterization of Their Interaction with Natural Nucleosides and Modified Arabinofuranoside Analogues.
biochemistry
mesophilic enzymes
modified nucleoside analogues
purine nucleoside phosphorylases
thermophilic enzymes
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
27 Aug 2024
27 Aug 2024
Historique:
received:
08
07
2024
revised:
20
08
2024
accepted:
21
08
2024
medline:
28
9
2024
pubmed:
28
9
2024
entrez:
28
9
2024
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 39334837
pii: biom14091069
doi: 10.3390/biom14091069
pii:
doi:
Substances chimiques
Purine-Nucleoside Phosphorylase
EC 2.4.2.1
Nucleosides
0
Bacterial Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : State assignment of Ministry of Science and Higher Education of the Russian Federation
ID : theme No. 1210-5260-0286