Thermodynamic and kinetic studies of competitive inhibition of adenosine deaminase by ring opened analogues of adenine nucleoside

Int J Biol Macromol. 1993 Apr;15(2):125-9. doi: 10.1016/0141-8130(93)90010-j.

Abstract

Ring opened analogues of adenine nucleosides substituted at the ninth adenine positions, with and without esterification (compounds I and II), have been studied kinetically and thermodynamically at various temperatures in order to determine the sites of ring opened analogues. These are deemed to be important for binding to the adenosine deaminase. Adenosine deaminase is found to bind more strongly to compound I than to compound II, therefore compound I is a stronger inhibitor than II, because the position of (5') OH on the ribose moiety decreases the inhibitory strength on the ring opened analogue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine / analogs & derivatives*
  • Adenosine / chemistry
  • Adenosine / pharmacology*
  • Adenosine Deaminase Inhibitors*
  • Animals
  • Binding, Competitive
  • Cattle
  • In Vitro Techniques
  • Kinetics
  • Structure-Activity Relationship
  • Thermodynamics

Substances

  • Adenosine Deaminase Inhibitors
  • Adenosine