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PROSITE documentation PDOC00557

Thymidine and pyrimidine-nucleoside phosphorylases signature





Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

THYMID_PHOSPHORYLASE, PS00647; Thymidine and pyrimidine-nucleoside phosphorylases signature  (PATTERN)


References

1AuthorsWalter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W., Krenitsky T.A., Ealick S.E.
TitleThree-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution.
SourceJ. Biol. Chem. 265:14016-14022(1990).
PubMed ID2199449

2AuthorsFurukawa T., Yoshimura A., Sumizawa T., Haraguchi M., Akiyama S.-I., Fukui K., Ishizawa M., Yamada Y.
TitleAngiogenic factor.
SourceNature 356:668-668(1992).
PubMed ID1570012
DOI10.1038/356668a0

3AuthorsSaxild H.H., Andersen L.N., Hammer K.
TitleDra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein.
SourceJ. Bacteriol. 178:424-434(1996).
PubMed ID8550462



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