Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin-Reference-Cited by-同舟云学术

Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin

Published:2007-07-17 Issue:2 Volume:37 Page:153-164
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

Modrak-Wójcik Anna,Kirilenko Aneta,Shugar David,Kierdaszuk Borys

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/s00249-007-0205-8.pdf

Reference62 articles.

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2. Behlke J, Koellner G, Bzowska A (2005) Oligomeric structure of mammalian purine nucleoside phosphorylase in solution determined by analytical ultracentrifugation. Z Naturforsch 60C:927–931

3. Bennett EM, Li C, Allan PW, Parker WB, Ealick SE (2003) Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase. J Biol Chem 278:47110–47118

4. Bzowska A, Kazimierczuk Z, Seela F (1998) 7-Deazapurine 2′-deoxyribofuranosides are noncleavable competitive inhibitors of Escherichia coli purine nucleoside phosphorylase (PNP). Acta Biochim Polon 45:755–768

5. Bzowska A, Kulikowska E, Shugar D (2000) Purine nucleoside phosphorylases: properties, functions, and clinical aspects. Pharmacol Ther 88:349–425

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