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
收藏
页码：21 / 28
页数：8
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