A1 Refereed original research article in a scientific journal
Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases
Authors: Moiseyev GP, Yakovlev GI, Lysov YP, Chernyi AA, Polyakov KM, Oivanen M, Lonnberg H, Beigelman LN, Efimtseva EV, Mikhailov SN
Publisher: ELSEVIER SCIENCE BV
Publication year: 1997
Journal:: FEBS Letters
Journal name in source: FEBS LETTERS
Journal acronym: FEBS LETT
Volume: 404
Issue: 2-3
First page : 169
Last page: 172
Number of pages: 4
ISSN: 0014-5793
DOI: https://doi.org/10.1016/S0014-5793(97)00092-6
Abstract
The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes, To this end the kinetic parameters of hydrolysis of UpA, 2'-C-Me- and 3'-C-Me-UpA were determined for RNase A, RNase Pb-2, nuclease S-1 and snake venom phosphodiesterase, In these derivatives the ranges of the allowed orientation of uridine residues are restricted due to the substitution of methyl groups for the ribose hydrogen atoms, The results described demonstrate that the proposed method is of general value for the estimation of the nucleotide glycoside angles in the productive enzyme-substrate complexes. (C) 1997 Federation of European Biochemical Societies.
The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes, To this end the kinetic parameters of hydrolysis of UpA, 2'-C-Me- and 3'-C-Me-UpA were determined for RNase A, RNase Pb-2, nuclease S-1 and snake venom phosphodiesterase, In these derivatives the ranges of the allowed orientation of uridine residues are restricted due to the substitution of methyl groups for the ribose hydrogen atoms, The results described demonstrate that the proposed method is of general value for the estimation of the nucleotide glycoside angles in the productive enzyme-substrate complexes. (C) 1997 Federation of European Biochemical Societies.