Stereoelectronic effects in RNase-catalysed reactions of dinucleoside phosphate cleavage.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Yakovlev GI,Bocharov AL,Moiseyev GP,Mikhaylov SN

doi

10.1016/0014-5793(85)80521-4

subject

Has Abstract

pub_date

1985-01-07 00:00:00

pages

217-20

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(85)80521-4

journal_volume

179

pub_type

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