Stereoelectronic effects in RNase-catalysed reactions of dinucleoside phosphate cleavage.
The rate at which dinucleoside phosphates are cleaved by RNases is supposed to be determined by the mole fraction of enzyme-substrate complexes in which the phosphodiester moiety of a dinucleoside phosphate has a highly reactive conformation. The mole fraction of such complexes for a particular RNase depends on the nature of a nucleoside at the O5'-end of the phosphodiester bond. Experimental data are presented to support this hypothesis.
D015226:Dinucleoside Phosphates; D007700:Kinetics; D008745:Methylation; D008968:Molecular Conformation; D009841:Oligonucleotides / Q000378:metabolism*; D010407:Penicillium / Q000201:enzymology; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism*; D013329:Structure-Activity Relationship
D015226:Dinucleoside Phosphates; D009841:Oligonucleotides; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic