Staphylococcal nuclease: size and specificity of the active site.
The dissociation constants and standard free energies of complex formation determined with staphylococcal nuclease and a series of 5'-phosphoryloligothymidyl derivatives of increasing chain length suggest that maximum stability is reached with an oligonucleotide containing three nucleotide units. A proposed model of the active site that contains other knowledge of the specificity and the catalytic mechanism of this enzyme postulates the existence of three nonequivalent phosphate binding subsites and a closely related phosphodiester hydrolytic subsite.
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D004247:DNA; D007700:Kinetics; D008956:Models, Chemical; D009596:Nitrophenols; D009711:Nucleotides; D010710:Phosphates; D010744:Phosphoric Monoester Hydrolases; D012313:RNA; D013210:Staphylococcus; D013936:Thymidine
D009596:Nitrophenols; D009711:Nucleotides; D010710:Phosphates; D012313:RNA; D004247:DNA; D010744:Phosphoric Monoester Hydrolases; D013936:Thymidine