|PROSITE documentation PDOC00557 [for PROSITE entry PS00647]|
Thymidine phosphorylase (EC 188.8.131.52) catalyzes the reversible phosphorolysis of thymidine, deoxyuridine and their analogues to their respective bases and 2-deoxyribose 1-phosphate. This enzyme regulates the availability of thymidine and is therefore essential to nucleic acid metabolism.
In Escherichia coli (gene deoA), the enzyme is a dimer of identical subunits of about 48 Kd . In humans it was first identified as platelet-derived endothelial cell growth factor (PD-ECGF) before being recognized  as thymidine phosphorylase.
As a signature pattern for these enzymes, we selected a well conserved region of 19 residues located in the N-terminal part of these proteins.Last update:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W., Krenitsky T.A., Ealick S.E.|
|Title||Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution.|
|Source||J. Biol. Chem. 265:14016-14022(1990).|
|2||Authors||Furukawa T., Yoshimura A., Sumizawa T., Haraguchi M., Akiyama S.-I., Fukui K., Ishizawa M., Yamada Y.|
|3||Authors||Saxild H.H., Andersen L.N., Hammer K.|
|Title||Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein.|
|Source||J. Bacteriol. 178:424-434(1996).|