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

共 12 条

[1] Substrate specificity of Escherichia coli thymidine phosphorylase
N. G. Panova
C. S. Alexeev
A. S. Kuzmichov
E. V. Shcheveleva
S. A. Gavryushov
K. M. Polyakov
A. M. Kritzyn
S. N. Mikhailov
R. S. Esipov
A. I. Miroshnikov
Biochemistry (Moscow), 2007, 72 : 21 - 28
[2] Substrate specificity of Escherichia coli thymidine phosphorylase
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.
BIOCHEMISTRY-MOSCOW, 2007, 72 (01) : 21 - 28
[3] Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity
Kurtis, Christian R. P.
Knowles, Peter F.
Parsons, Mark R.
Gaule, Thembaninkosi G.
Phillips, Simon E. V.
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JOURNAL OF NEURAL TRANSMISSION, 2011, 118 (07) : 1043 - 1053
[4] Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity
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Peter F. Knowles
Mark R. Parsons
Thembaninkosi G. Gaule
Simon E. V. Phillips
Michael J. McPherson
Journal of Neural Transmission, 2011, 118 : 1043 - 1053
[5] Substrate specificity of E-coli uridine phosphorylase. Further evidences of high-syn conformation of the substrate in uridine phosphorolysis
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Sivets, G. G.
Safonova, T. N.
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[6] Reengineering substrate specificity of E. coli glutamate dehydrogenase using a position-based prediction method
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Biotechnology Letters, 2017, 39 : 599 - 605
[7] Ribokinase from E-coli:: Expression, purification, and substrate specificity
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Muravyova, Tatyana I.
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JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2011, 72 (3-4) : 95 - 101
[9] Reengineering substrate specificity of E-coli glutamate dehydrogenase using a position-based prediction method
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BIOTECHNOLOGY LETTERS, 2017, 39 (04) : 599 - 605
[10] Investigating the role of the hydroxyl groups of substrate erythrose 4-phosphate in the reaction catalysed by the first enzyme of the shikimate pathway
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Pietersma, Amy L.
Schofield, Linley R.
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BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2011, 21 (22) : 6838 - 6841

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