Substrate specificity of Escherichia coli thymidine phosphorylase

被引：19

作者：

Panova, N. G.

Alexeev, C. S.

Kuzmichov, A. S.

Shcheveleva, E. V.

Gavryushov, S. A.

Polyakov, K. M.

Kritzyn, A. M.

Mikhailov, S. N.

Esipov, R. S.

Miroshnikov, A. I.

机构：

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

[2] Russian Acad Sci, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2007年 / 72卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

thymidine phosphorylase; thymidine derivatives; substrate specificity; inhibitors; analysis in terms of steric interactions;

D O I：

10.1134/S0006297907010026

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 Escherichia coli thymidine phosphorylase to thymidine derivatives modified at 5'-, 3'-, and 2',3'-positions of the sugar moiety was studied. Equilibrium and kinetic constants (K (m), K (I), k (cat)) of the phosphorolysis reaction have been determined for 20 thymidine analogs. The results are compared with X-ray and molecular dynamics data. The most important hydrogen bonds in the enzyme-substrate complex are revealed.

引用

页码：21 / 28

页数：8

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