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Synthesis of (14C)-Ribose-5-Phosphate and (14C)-Phosphoribosyl-Pyrophosphate and Their use in New Enzyme Assays

  • Gerry R. Boss
  • Soha D. Idriss
  • Randall C. Willis
  • J. E. Seegmiller
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 165)

Abstract

Phosphoribosylpyrophosphate (PP-ribose-P) is a specific substrate for eight synthetic enzymes in mammalian cells (1). Three of these enzymes, glutamine phosphoribosylpyrophosphate amidotrans-ferase (PP-ribose-P amidotransferase, (EC.2.4.2.14), hypoxanthine-guanine phosphoribosyltransferase (HPRT, EC.2.4.2.8) and adenine phosphoribosyltransferase (APRT, EC.2.4.2.7) are required for purine nucleotide synthesis and one, orotate phosphoribosyltransferase (OPRT, EC.2.4.2.10) for pyrimidine nucleotide synthesis. Since PP-ribose-P serves not only as a substrate of PP-ribose-P amido-transferase, but also as an allosteric regulator of activity (2), the intracellular concentration of PP-ribose-P appears to be a major determinant of purine nucleotide synthesis. The immediate precursor of PP-ribose-P is ribose-5-phosphate (ribose-5-P).

Keywords

Synthetase Activity Purine Metabolism Allosteric Regulator Nucleotide Synthesis Synthetic Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Gerry R. Boss
    • 1
  • Soha D. Idriss
    • 1
  • Randall C. Willis
    • 1
  • J. E. Seegmiller
    • 1
  1. 1.Department of MedicineUniversity of CaliforniaSan Diego, La JollaUSA

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