- Structures of native human thymidine phosphorylase and in complex with 5-iodouracil.
Structures of native human thymidine phosphorylase and in complex with 5-iodouracil.
Biochemical and biophysical research communications (2009-06-27)
Eirini Mitsiki, Anastassios C Papageorgiou, Shalini Iyer, Nethaji Thiyagarajan, Steven H Prior, Darrell Sleep, Chris Finnis, K Ravi Acharya
PMID19555658
ABSTRACT
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 2.5A, respectively. In addition, we provide information on the role of specific residues in the enzymatic activity of hTP through mutagenesis and kinetic studies.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Thymidine Phosphorylase, recombinant from Escherichia coli, recombinant, expressed in E. coli, buffered aqueous solution, ≥900 units/mL, 0.2 μm filtered
Sigma-Aldrich
Thymidine Phosphorylase, recombinant from Escherichia coli, recombinant, expressed in E. coli, buffered aqueous solution, ≥500 units/mL
Sigma-Aldrich
Thymidine Phosphorylase, recombinant from Escherichia coli, recombinant, expressed in E. coli, Suitable for manufacturing of diagnostic kits and reagents, buffered aqueous solution, ≥500 units/mL