Hypotensive activity of two benzothiadiazine derivatives

✍ Scribed by Albert I. Edlin; William J. Kinnard; Eugene E. Vogin; Joseph P. Buckley

• Publisher: John Wiley and Sons
• Year: 1965
• Tongue: English
• Weight: 486 KB
• Volume: 54
• Category: Article
• ISSN: 0022-3549
• DOI: 10.1002/jps.2600540106

✦ Synopsis

Finally, it is apparent that the stereochemistry of the substituent on the 9-position of the purine nucleus can vary considerably from that of ribose without appreciably affecting binding to the enzyme. For example, in the present case, the hydroxy group a t CS, is absent, and the hydroxy group at C,, is in the opposite configuration than found in the normal substrate, adenosine. These results support the previously stated view that the active site of adenosine deaminase has a large bulk tolerance in the area where the 9-substituent of adenosine analogs bind (6). Furthermore, an inspection of molecular models shows that the hydrogen of the Carhydroxy group of the 5-deoxyxylofuranosylpurines can occupy an almost identical position as the hydrogen of the C6,-hydroxy group in one of the conformations of adenosine. It, therefore, is possible that in compounds like IX, X, and XI11 the hydrogen of the Ca*-hydroxy group is bound to the enzyme at that position where the hydrogen of the C6*-hydroxy group of adenosine would be bound normally.