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Peer-reviewedCC BY 4.0International Journal of Molecular Sciences

The Effects of the Medium’s pH Value on the Efficiency of the Enzymatic Transglycosylation Catalyzed by Escherichia coli Purine Nucleoside Phosphorylase and Lactobacillus leichmanii Nucleoside Deoxyribosyltransferase Type II

  1. 1Laboratory of the Design and Synthesis of Biologically Active Compounds, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str. 32, 119991 Moscow, Russia
  2. 2Laboratory of Molecular Basis of Action of Physiologically Active Compounds, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str. 32, 119991 Moscow, Russia

Abstract

The effect of the reaction medium pH value on the rate and yield of enzymatic transglycosylation catalyzed by Escherichia coli purine nucleoside phosphorylase (EcPNP) and Lactobacillus leichmanii type II nucleoside deoxyribosyltransferase (LlNDTII) was investigated. In the presence of EcPNP at pH 5.5, a significant reduction in the inosine formation rate was observed, compared with that of adenosine. A substituent at the purine O6 position neutralizes the negative effect of the 6-oxo group on the reaction rate. A substituent at the purine N6 position has virtually no effect on the transglycosylation rate. In reactions catalyzed by LlNDTII, the rate of nucleoside formation from 4-oxopyrimidines was higher at pH 5.5, but the yield decreased by approximately 10% compared with that at pH 7.0; an unusual dependence of the yield of the target nucleoside on the enzyme concentration used was also revealed.

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BibTeX
@article{alexeev2026effects,
  title = {{The Effects of the Medium’s pH Value on the Efficiency of the Enzymatic Transglycosylation Catalyzed by Escherichia coli Purine Nucleoside Phosphorylase and Lactobacillus leichmanii Nucleoside Deoxyribosyltransferase Type II}},
  author = {Cyril S. Alexeev and Maria A. Konkina and Ivan A. Oskolsky and Dmitrii A. Platov and Mikhail S. Drenichev},
  journal = {International Journal of Molecular Sciences},
  year = {2026},
  month = nov,
  doi = {10.3390/ijms27219901},
  url = {https://www.mdpi.com/1422-0067/27/21/9901},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - The Effects of the Medium’s pH Value on the Efficiency of the Enzymatic Transglycosylation Catalyzed by Escherichia coli Purine Nucleoside Phosphorylase and Lactobacillus leichmanii Nucleoside Deoxyribosyltransferase Type II
AU  - Cyril S. Alexeev
AU  - Maria A. Konkina
AU  - Ivan A. Oskolsky
AU  - Dmitrii A. Platov
AU  - Mikhail S. Drenichev
PY  - 2026
DA  - 2026/11/05
JO  - International Journal of Molecular Sciences
DO  - 10.3390/ijms27219901
UR  - https://www.mdpi.com/1422-0067/27/21/9901
AB  - The effect of the reaction medium pH value on the rate and yield of enzymatic transglycosylation catalyzed by Escherichia coli purine nucleoside phosphorylase (EcPNP) and Lactobacillus leichmanii type II nucleoside deoxyribosyltransferase (LlNDTII) was investigated. In the presence of EcPNP at pH 5.5, a significant reduction in the inosine formation rate was observed, compared with that of adenosine. A substituent at the purine O6 position neutralizes the negative effect of the 6-oxo group on the reaction rate. A substituent at the purine N6 position has virtually no effect on the transglycosylation rate. In reactions catalyzed by LlNDTII, the rate of nucleoside formation from 4-oxopyrimidines was higher at pH 5.5, but the yield decreased by approximately 10% compared with that at pH 7.0; an unusual dependence of the yield of the target nucleoside on the enzyme concentration used was also revealed.
SN  - 1422-0067
ER  -