EC Number |
---|
2.4.2.4 | - |
2.4.2.4 | analysis of crystal structure of recombinant Escherichia coli TP in complex with 2'-fluoro-3'-azido-2',3'-dideoxyuridine (N3FddU) and 3'-azidothymidine (AZT) at 1.50 A and 1.52 A resolutions, respectively. Analysis of the free enzyme crystal structure at 2.8 A resolution |
2.4.2.4 | analysis of crystal structure of recombinant human TP in complex with 5-iodouracil (5IUR) at 3.0 A and 2.5 A resolutions, respectively |
2.4.2.4 | enzyme complexed with TPI |
2.4.2.4 | hanging drop vapor diffusion method |
2.4.2.4 | purified recombinant thymidine phosphorylase, free and in complex with 5-iodouracil, X-ray diffraction structure determination and analysis at 3.0 A and 2.5 A resolutions, respectively |
2.4.2.4 | sitting drop vapor diffusion method, using 0.2 M potassium thiocyanate, 0.1 M bis-Tris propane, 20% (w/v) PEG 3350 pH 7.5 (unliganded enzyme), or 0.1 M Bicine, 1.6 M (NH4)2SO4 pH 9.0 (in complex with thymidine), or 0.1 M citric acid, 10% (w/v) PEG 6000 pH 5.0 (in complex with uridine) |
2.4.2.4 | structure of enzyme from crystals grown in the presence of thymidine |
2.4.2.4 | structure of HTP bound to the small molecule inhibitor 5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil hydrochloride, glutathione S-transferase fused to thymidine phosphorylase residues 12482 (based on Swissprot accession number P19971) via a thrombin-cleavable linker, crystallizationd at 15°C using the hanging-drop vapor method |
2.4.2.4 | X-ray diffraction structure determination and analysis of the free enzyme at 3.5 A resolution, and of the in complex with the small and potent inhibitor 5-chloro-6-[1-(2-iminopyrrolidinyl)methyl] uracil at 2.1 A resolution |