Steric and charge factors in the resistance of uridylyl(3' - 5')N6-(N-threonylcarbonyl)adenosine to venom phosphodiesterase hydrolysis.
The contribution of steric and negative charge factors to the resistance of uridylyl(3' - 5')N6-(N-threonylcarbonyl)adenosine to venom phosphodiesterase was investigated. The hydrolysis rates of uridylyl(3'-5')N6-(N-threonylcarbonyl)-adenosine, its model derivatives, methyl ester and O-benzyl ester, together with unmodified uridyly (3'-5')adenosine, were studied. It was found that the contribution of both factors is of the same order. The steric inhibition of digestion is distinctly higher than that confirmed by N6-(delta2-isopentenyl)adenosine [1], which is ascribed to the rigid conformation of the threonylcarbonyladenosine side chain.
D000241:Adenosine / Q000031:analogs & derivatives*; D007700:Kinetics; D008968:Molecular Conformation; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D012910:Snake Venoms; D013329:Structure-Activity Relationship; D014500:Uracil Nucleotides / Q000031:analogs & derivatives; D014542:Uridine Monophosphate / Q000031:analogs & derivatives
D012910:Snake Venoms; D014500:Uracil Nucleotides; D014542:Uridine Monophosphate; D010727:Phosphoric Diester Hydrolases; D000241:Adenosine