Nonclassical Antimetabolites XIX: Simulation of 5′-Phosphoribosyl Binding III. Relative Contribution of Phosphate and the Other Oxygen-Containing Functions to the Binding of the 5′-Phosphoribosyl Moiety to Succinoadenylate Kinosynthetase

Abstract

The synthesis of 6-mercapto-9H-purine-9-yl-pentanol phosphate (VI) and 9H-adenine-9-yl-pentanol phosphate (VII) <i>via</i> 5-amino-4-chloro-6-(5′-hydroxypentyl-amino)pyrimidine (X) are described. The comparison of VI, VII, thioinosinic acid (III), 5′-adenylic acid (IV), 2′-deoxy-5′-adenylic acid (V), thioinosine (XIII), and adenosine as inhibitors of succinoadenylate kinosynthetase indicated that the twelvefold decrease in activity of VI and VII compared to the ribonucleotides, VII and IV, was due primarily to the removal of the 2′-hydroxyl group and not the 3′-hydroxyl or furanosyl oxygen group of the ribosyl moiety.