Biochemistry (Mosc), 2007, 72(1):21-28

Substrate specificity of Escherichia coli thymidine phosphorylase

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 (Km, KI, kcat) 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. © Nauka/Interperiodica 2007.

Panova NG, Alexeev CS, Kuzmichov AS, Shcheveleva EV, Gavryushov SA, Polyakov KM, Kritzyn AM, Mikhailov SN, Esipov RS, Miroshnikov AI

IBCH: 743
Ссылка на статью в журнале: http://link.springer.com/10.1134/S0006297907010026
Кол-во цитирований на 10.2023: 20
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