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 RNas...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1985-01, Vol.179 (2), p.217-220
Main Authors: Yakovlev, Gennady I., Bocharov, Alexander L., Moiseyev, Gennady P., Mikhaylov, Sergey N.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Dinucleoside Phosphates
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Kinetics
Methylation
Molecular Conformation
Oligonucleotides - metabolism
Penicillium - enzymology
phosphodiester bonds
ribonuclease (pancreatic)
Ribonuclease, Pancreatic - metabolism
Ribonucleases - metabolism
RNase
Stereoelectronic control specificity
Structure-Activity Relationship
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)80521-4