Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases



: Moiseyev GP, Yakovlev GI, Lysov YP, Chernyi AA, Polyakov KM, Oivanen M, Lonnberg H, Beigelman LN, Efimtseva EV, Mikhailov SN

Publisher: ELSEVIER SCIENCE BV

: 1997

: FEBS Letters

: FEBS LETTERS

: FEBS LETT

: 404

: 2-3

: 169

: 172

: 4

: 0014-5793

DOI: https://doi.org/10.1016/S0014-5793(97)00092-6


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.



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