PROSITE documentation PDOC00557
Thymidine and pyrimidine-nucleoside phosphorylases signature


Thymidine phosphorylase (EC 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 (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)


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

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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