| Literature DB >> 17309433 |
N G Panova1, 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.
Abstract
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.Entities:
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Year: 2007 PMID： 17309433 DOI： 10.1134/s0006297907010026
Source DB: PubMed Journal: Biochemistry (Mosc) ISSN： 0006-2979 Impact factor: 2.487