Substrate Specificity of Thymidine Phosphorylase of E. Coli: Role of Hydroxyl Groups

被引：5

作者：

Panova, Natalya G. ^{[1
]}

Alexeev, Cyril S. ^{[1
]}

Polyakov, Konstantin M. ^{[1
]}

Gavryushov, Sergei A. ^{[1
]}

Kritzyn, Anatoliy M. ^{[1
]}

Mikhailov, Sergey N. ^{[1
]}

机构：

[1] Russian Acad Sci, VA Engelhardt Mol Biol Inst, Moscow 119991, Russia

来源：

NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS | 2008年 / 27卷 / 12期

基金：

俄罗斯基础研究基金会;

关键词：

Thymidine phosphorlase; substrate specificity; thymidine derivatives;

D O I：

10.1080/15257770802257895

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：

Substrate specificity of E. coli thymidine phosphorylase to pyrimidine nucleoside modified at 5 '-, 3 '-, and 2 '-positions of sugar moiety has been studied. Equilibrium (Keq) and kinetics constants of phosphorolysis reaction of nucleosides were measured. The most important hydrogen bonds in enzyme-substrate complex have been determined.

引用

页码：1211 / 1214

页数：4

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