Structures of native human thymidine phosphorylase and in complex with 5-iodouracil
| Autor: | K. R. Acharya, Anastassios C. Papageorgiou, Stephen H. Prior, Darrell Sleep, E Mitsiki, Nethaji Thiyagarajan, Shalini Iyer, C Finnis |
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| Rok vydání: | 2009 |
| Předmět: |
Protein Conformation
Angiogenesis Biophysics Crystallography X-Ray Biochemistry Article Phosphates law.invention 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine law Humans Transferase 5-Iodouracil Enzyme kinetics Thymidine phosphorylase Uracil Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Crystal structure Mutagenesis Cell Biology Molecular biology 3. Good health Enzyme chemistry 030220 oncology & carcinogenesis Mutation Recombinant DNA |
| Zdroj: | Biochemical and Biophysical Research Communications |
| ISSN: | 0006-291X |
| Popis: | Thymidine phosphorylase (TP) first identified as platelet derived endothelial cell growth factor (PD-ECGF) plays a key role in nucleoside metabolism. Human TP (hTP) is implicated in angiogenesis and is overexpressed in several solid tumors. Here, we report the crystal structures of recombinant hTP and its complex with a substrate 5-iodouracil (5IUR) at 3.0 and 2.5Å, respectively. In addition, we provide information on the role of specific residues in the enzymatic activity of hTP through mutagenesis and kinetic studies. |
| Databáze: | OpenAIRE |
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