Species differences in substrate specificity of pyrimidine nucleoside phosphorylase

Yoshihiko Maehara, Yoshihisa Sakaguchi, Tetsuya Kusumoto, Hiroki Kusumoto, Keizo Sugimachi

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


To compare the activity of pyrimidine nucleoside phosphorylase (PNP), an enzyme involved in the metabolism of 5‐fluorouracil (5‐FU), we used uridine (Urd), deoxyuridine (dUrd), and thymidine (dThd) as substrates and human, rat, and mouse neoplastic and normal tissues. As PNP activity was higher in the tumor tissues than in the normal ones in all species examined, the level of PNP activity is expected to be one critical factor linked to the effectiveness of 5‐FU. In rats and mice, the ratio of the activities of Urd, dUrd, and dThd was about 10:7:1, whereas in humans, the ratio was 1:30:20. The main enzyme of PNP is Urd phosphorylase in rodents and dThd phosphorylase in humans. Therefore, when examining the metabolism of 5‐FU and its analogues for potential clinical application, human tissues should be used.

Original languageEnglish
Pages (from-to)184-186
Number of pages3
JournalJournal of Surgical Oncology
Issue number3
Publication statusPublished - Nov 1989
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Surgery
  • Oncology


Dive into the research topics of 'Species differences in substrate specificity of pyrimidine nucleoside phosphorylase'. Together they form a unique fingerprint.

Cite this