COMPARISON OF ACID-CATALYZED AND ENZYME-CATALYZED CLEAVAGE OF THE GLYCOSIDIC BOND OF N(7)-SUBSTITUTED GUANOSINES

被引：4

作者：

BZOWSKA, A

KULIKOWSKA, E

SHUGAR, D

机构：

[1] Department of Biophysics, University of Warsaw, 02-089, Warsaw

来源：

NUCLEOSIDES & NUCLEOTIDES | 1990年 / 9卷 / 03期

关键词：

D O I：

10.1080/07328319008045164

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Kinetic parametrs for enzymatic cleavage of the glycosidic bond (phosphorolysis) of ten N(7)-substituted guanosines were determined, and used to establish a structure-activity relation for the Michaelis constants. Results were compared with those for acid-catalyzed cleavage of the glycosidic bonds, and are consistent with a mechanism for phosphorolysisvia protonation of the purine ring N(7). © 1990, Taylor & Francis Group, LLC. All rights reserved.

引用

页码：439 / 440

页数：2

共 7 条

[1]

BZOWSKA A, 1988, J BIOL CHEM, V263, P9212

[2]

DARZYNKIEWICZ E, 1989, IN PRESS BIOCHEM

[3] AROMATIC SUBSTITUENT CONSTANTS FOR STRUCTURE-ACTIVITY CORRELATIONS [J].