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Symmetric Nucleosides as Potent Purine Nucleoside Phosphorylase Inhibitors

The Journal of Physical Chemistry B, 2021
Nucleic acids are one of the most enigmatic biomolecules crucial to several biological processes. Nucleic acid-protein interactions are vital for the coordinated and controlled functioning of a cell, leading to the design of several nucleoside/nucleotide analogues capable of mimicking these interactions and hold paramount importance in the field of ...
Pradeep Pant, Amita Pathak, B. Jayaram
openaire   +2 more sources

The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27

Journal of Biomolecular Structure and Dynamics, 2020
Two recombinant purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27 encoded by genes TT_C1070 (TthPNPI) and TT_C0194 (TthPNPII) were purified and characterized.
V. Timofeev   +10 more
semanticscholar   +1 more source

Biocatalytic synthesis of seleno-, thio- and chloro-nucleobase modified nucleosides by thermostable nucleoside phosphorylases

Catalysis communications, 2019
Selenium-containing nucleosides are the building blocks of the Se-nucleic acids useful for structure-and-function study, drug discovery and for targeting nucleic acids and their protein complexes.
Xinrui Zhou   +6 more
semanticscholar   +1 more source

Use of nucleoside phosphorylases for the preparation of 5-modified pyrimidine ribonucleosides.

Biochimica et Biophysica Acta - Proteins and Proteomics, 2019
Enzymatic transglycosylation, a transfer of the carbohydrate moiety from one heterocyclic base to another, is catalyzed by nucleoside phosphorylases (NPs) and is being actively developed and applied for the synthesis of biologically important nucleosides.
C. S. Alexeev   +5 more
semanticscholar   +1 more source

Chemo-enzymatic synthesis of α-d-pentofuranose-1-phosphates using thermostable pyrimidine nucleoside phosphorylases

Molecular Catalysis, 2018
α- d -pentofuranose-1-phosphates (Pentose-1Ps) are key intermediates in nucleoside metabolism and important precursors for the enzymatic synthesis of modified nucleosides.
Sarah Kamel   +5 more
semanticscholar   +1 more source

Enzymatic Synthesis of Nucleoside Analogues by Nucleoside Phosphorylases

Enzymatic and Chemical Synthesis of Nucleic Acid Derivatives, 2018
Nucleosides primarily consist of a nitrogenous base (nucleobase), which is either a purine base or a pyrimidine base and a five-carbon sugar (pentose). The base and sugar are covalently linked via an N-glycosidic bond (Figure 1.1).
Sarah Kamel   +3 more
semanticscholar   +1 more source

Biosynthesis of nucleoside analogues via thermostable nucleoside phosphorylase

Applied Microbiology and Biotechnology, 2012
Biocatalyzed synthesis of nucleoside analogues was carried out using two thermostable nucleoside phosphorylases from the hyperthermophilic aerobic crenarchaeon Aeropyrum pernix K1. The synthesis of the 2,6-diaminopurine nucleoside and 5-methyluridine was used as a reaction model to test the process.
Shaozhou, Zhu   +6 more
openaire   +2 more sources

LINGCOD MUSCLE PURINE NUCLEOSIDE PHOSPHORYLASE

Canadian Journal of Biochemistry and Physiology, 1958
A purine nucleoside phosphorylase enzyme preparation, which catalyzed the general reaction ribose (deoxyribose) [Formula: see text] nucleoside (deoxynucleoside)+orthophosphate, was isolated from muscles of the lingcod (Ophiodon elongatus). The reaction was found to be about 85% in favor of nucleoside synthesis with 10 μM./ml.
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Vanadate as a new substrate for nucleoside phosphorylases

JBIC Journal of Biological Inorganic Chemistry, 2022
A. Antipov   +3 more
semanticscholar   +1 more source

Purine nucleoside phosphorylase of chicken liver

Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
Abstract Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyltransferase, EC 2.4.2.1) has been purified 125-fold from the homogenate of chicken livers and some of the properties of the purified enzyme have been studied. This enzyme had a pH optimum at around 6.o. At high substrate levels of inosine the reaction rate was increased,
K, Murakami, A, Mitsui, K, Tsushima
openaire   +2 more sources

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