Substrate Specificity of a Thymidine Phosphorylase in Human Liver Tumor

Akira Kono, Yasuhiro Hara, Setsuro Sugata, Yoshikazu Matsushima, Tohru Ueda

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)


A thymidine phosphorylase preparation was partially purified from human liver tumor tissues (poorly differentiated adenocarcinoma). The substrate specificity of the enzyme was investigated with eleven pyrimidine nucleosides. Thymidine and 2`-deoxyuridine were good substrates, while uridine, 3’-deoxyuridine, 5’-deoxyuridine and 2’,3’-dideoxy-3’-hydroxy-methyluridine were not. Uridines substituted at the 5-position by a cyano, bromo, or chloro group were also phosphorolyzed by the enzyme, but the activity for 5-fluorouridine was much lower. 5’-Deoxy-5-fluorouridine was also cleaved. Either a 5-substituent or a 2’-deoxy structure seems to be essential for a good substrate.

Original languageEnglish
Pages (from-to)1919-1921
Number of pages3
JournalChemical and Pharmaceutical Bulletin
Issue number5
Publication statusPublished - 1984


  • 5’-deoxy-5-fluorouridine
  • deoxvuridine
  • human tumor
  • liver cancer
  • substrate specificity
  • thymidine
  • thymidine phosphorylase
  • uridine
  • uridine 5-substituted
  • uridine phosphorylase

ASJC Scopus subject areas

  • General Chemistry
  • Drug Discovery


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