PROSITE documentation PDOC00557Thymidine and pyrimidine-nucleoside phosphorylases signature
Thymidine phosphorylase (EC 2.4.2.4) 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 [1]. In humans it was first identified as platelet-derived endothelial cell growth factor (PD-ECGF) before being recognized [2] as thymidine phosphorylase.
Bacterial pyrimidine-nucleoside phosphorylase (EC 2.4.2.2) (gene pdp) [3] is an enzyme evolutionary and structurally related to 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.
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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). | |
| PubMed ID | 2199449 |
| 2 | Authors | Furukawa T. Yoshimura A. Sumizawa T. Haraguchi M. Akiyama S.-I. Fukui K. Ishizawa M. Yamada Y. |
| Title | Angiogenic factor. | |
| Source | Nature 356:668-668(1992). | |
| PubMed ID | 1570012 | |
| DOI | 10.1038/356668a0 |
| 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). | |
| PubMed ID | 8550462 |
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