These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Substrate specificity of Escherichia coli thymidine phosphorylase.
    Author: Panova NG, Alexeev CS, Kuzmichov AS, Shcheveleva EV, Gavryushov SA, Polyakov KM, Kritzyn AM, Mikhailov SN, Esipov RS, Miroshnikov AI.
    Journal: Biochemistry (Mosc); 2007 Jan; 72(1):21-8. PubMed ID: 17309433.
    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.
    [Abstract] [Full Text] [Related] [New Search]