In vitro recycling of alpha-D-ribose 1-phosphate for the salvage of purine bases

Biochim Biophys Acta. 2000 Mar 6;1474(1):70-4. doi: 10.1016/s0304-4165(99)00217-2.

Abstract

In this paper, we extend our previous observation on the mobilization of the ribose moiety from a purine nucleoside to a pyrimidine base, with subsequent pyrimidine nucleotides formation (Cappiello et al., Biochim. Biophys. Acta 1425 (1998) 273-281). The data show that, at least in vitro, also the reverse process is possible. In rat brain extracts, the activated ribose, stemming from uridine as ribose 1-phosphate, can be used to salvage adenine and hypoxanthine to their respective nucleotides. Since the salvage of purine bases is a 5-phosphoribosyl 1-pyrophosphate-dependent process, catalyzed by adenine phosphoribosyltransferase and hypoxanthine guanine phosphoribosyltransferase, our results imply that Rib-1P must be transformed into 5-phosphoribosyl 1-pyrophosphate, via the successive action of phosphopentomutase and 5-phosphoribosyl 1-pyrophosphate synthetase; and,in fact, no adenosine could be found as an intermediate when rat brain extracts were incubated with adenine, Rib-1P and ATP, showing that adenine salvage does not imply adenine ribosylation, followed by adenosine phosphorylation. Taken together with our previous results on the Rib-1P-dependent salvage of pyrimidine nucleotides, our results give a clear picture of the in vitro Rib-1P recycling, for both purine and pyrimidine salvage.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain / metabolism*
  • In Vitro Techniques
  • Male
  • Phosphoribosyl Pyrophosphate / metabolism*
  • Phosphotransferases / metabolism
  • Purines / metabolism*
  • Pyrimidine Nucleotides / metabolism
  • Rats
  • Rats, Wistar
  • Ribosemonophosphates / metabolism*
  • Substrate Cycling

Substances

  • Purines
  • Pyrimidine Nucleotides
  • Ribosemonophosphates
  • ribose 1-phosphate
  • Phosphoribosyl Pyrophosphate
  • Phosphotransferases
  • phosphopentomutase