Further studies on the substrate specificity of calf spleen phosphodiesterase [EC 3.1.4.18].
The synthesis of 5'-deoxy-5'-chlorothymidine-3'-(4-nitrophenyl)phosphate (5) and 5'-deoxy-5'-chlorothymidine-3'-(4-nitrophenyl)phosphorothioate (6) via corresponding phosphoranilidodiester intermediate is described. The affinity of 5 and 6 towards SPDE in comparison with thymidine-3'-(4-nitrophenyl)phosphate is tested. These findings reveal that the presence of 5'-hydroxyl function in the substrate is not necessary for hydrolytic action of this enzyme.
D000818:Animals; D002417:Cattle; D005092:Exonucleases / Q000378:metabolism*; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity; D013873:Thionucleotides / Q000138:chemical synthesis*; D013938:Thymidine Monophosphate / Q000031:analogs & derivatives / Q000138:chemical synthesis*; D013942:Thymine Nucleotides / Q000138:chemical synthesis*
D013873:Thionucleotides; D013942:Thymine Nucleotides; D013938:Thymidine Monophosphate; C032452:5'-deoxy-5'-chlorothymidine 3'-(4-nitrophenyl)phosphate; C032453:5'-deoxy-5'-chlorothymidine-3'-(4-nitrophenyl)phosphorothioate; D005092:Exonucleases; C022650:spleen exonuclease