Pyrimidine Nucleoside Phosphorylase

Pyrimidine Nucleoside Phosphorylase Catalog Number: B2017876 (1 mL)

Scientific Description

Pyrimidine Nucleoside Phosphorylase (PYNP), supplied as a ready-to-use solution (Catalog B2017876, 1 mL), catalyzes the reversible phosphorolysis of pyrimidine nucleosides into their corresponding pyrimidine bases and -D-ribose-1-phosphate. With no molecular weight specified, the enzyme is provided in a biotechnology-grade formulationultrapure and sterilethat supports laboratory workflows requiring high fidelity and traceability. Storage at 20 C ensures enzyme integrity over repeated freeze-thaw cycles, making it ideal for routine and advanced enzymology workflows.

In research, this enzyme plays an important role in exploring nucleotide salvage pathways, as it efficiently recycles pyrimidine nucleosides for nucleotide synthesis. Widely applied across biochemical, chemical, and immunological assays, its soluble format facilitates seamless integration into kinetic studies, substrate screening, and pathway validation protocols. The solution format also enables precise volume-based dispensing, which is especially beneficial for high-throughput and multi-well applications.

Researchers frequently employ PYNP in designing salvage pathway models, optimizing reaction conditions to favor either phosphorolytic or synthetic directions, and in constructing educational modules illustrating enzymatic nucleotide transformations. Its clean documentation, defined volume, and compatible storage conditions make it a reliable reagent for standard operating procedures, inventory systems, and collaborative multi-user environments.

Why researchers choose this product:

• Ready-to-use 1 mL solution simplifies dosing and eliminates reconstitution steps
• Efficiently catalyzes phosphorolysis of pyrimidine nucleosides, aiding salvage-pathway and metabolism research
• Biotechnology-grade purity ensures compatibility with sensitive assays and sterile workflows
• Stable at 20 C for robust cold-chain handling and consistent performance

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.

References

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• 2: Kaspar F, Neubauer P, Kurreck A. The Peculiar Case of the Hyper-thermostable Pyrimidine Nucleoside Phosphorylase from Thermus thermophilus* Chembiochem. 2021 Apr 16;22(8):1385-1390.
• 3: Wen Y, Li X, Guo W, Wu B. Crystal structures of a new class of pyrimidine/purine nucleoside phosphorylase revealed a Cupin fold Proteins. 2022 Jun;90(6):1233-1241.
• 4: Vande Voorde J, Liekens S, Gago F, Balzarini J. The pyrimidine nucleoside phosphorylase of Mycoplasma hyorhinis and how it may affect nucleoside-based therapy Nucleosides Nucleotides Nucleic Acids. 2014;33(4-6):394-402.
• 5: Balaev VV, Prokofev II, Gabdoulkhakov AG, Betzel C, Lashkov AA. Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):193-197.
• 6: Liu K, Zhou Y, Zhang J, Chu J, Zhang Y, He B. A thermostable pyrimidine_nucleoside phosphorylase from Brevibacillus borstelensis LK01 for synthesizing halogenated nucleosides Biotechnol Lett. 2017 Dec;39(12):1903-1910.
• 7: Higley B, Oakes J, De Mello J, Giles GR. Pyrimidine_nucleoside phosphorylase activity in tumour and matched normal gastrointestinal mucosa Gut. 1982 Dec;23(12):1072-6.
• 8: Kaspar F, Wolff DS, Neubauer P, Kurreck A, Arcus VL. pH-Independent Heat Capacity Changes during Phosphorolysis Catalyzed by the Pyrimidine_Nucleoside Phosphorylase from Geobacillus thermoglucosidasius Biochemistry. 2021 May 25;60(20):1573-1577.
• 9: Liu G, Wang J, Chu J, Jiang T, Qin S, Gao Z, He B. Engineering Substrate Promiscuity of Nucleoside Phosphorylase Via an Insertions-Deletions Strategy JACS Au. 2024 Jan 13;4(2):454-464.
• 10: Vande Voorde J, Gago F, Vrancken K, Liekens S, Balzarini J. Characterization of pyrimidine nucleoside phosphorylase of Mycoplasma hyorhinis: implications for the clinical efficacy of nucleoside analogues Biochem J. 2012 Jul 1;445(1):113-23.