Production of Adenosine and Nucleoside Analogues by an Exchange Reaction Catalyzed by Adenosine Kinase

  • Mohsine Mimouni
  • Françoise Bontemps
  • Georges Van den Berghe
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 370)

Abstract

We have shown previously that rat liver adenosine kinase can catalyze an exchange reaction between adenosine (Ado) and AMP in the absence of ATP (1). This exchange reaction was potently stimulated by ADP. When measured in the absence of added ADP, the exchange could be due to a slight (0.001 %) contamination by ADP of analytical grade AMP (2). The ADP requirement of the Ado-AMP exchange intervenes in an ordered Bi Bi mechanism in which ATP is the first substrate to bind to the enzyme, and ADP the last product to dissociate. In the present work we have investigated (i) if Ado or AMP could be replaced by, respectively, nucleoside or nucleoside monophosphate analogs and (ii) if the Ado-AMP exchange is restricted to liver.

Keywords

Exchange Reaction Human Erythrocyte Analog Nucleoside Adenylate Kinase Adenosine Kinase 
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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Mohsine Mimouni
    • 1
  • Françoise Bontemps
    • 1
  • Georges Van den Berghe
    • 1
  1. 1.Laboratory of Physiological Chemistry, International Institute of Cellular and Molecular PathologyUniversity of Louvain Medical SchoolBrusselsBelgium

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