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PROSITE documentation PDOC00946

Purine and other phosphorylases family 1 signature




Description

The following phosphorylases belongs to the same family:

  • Purine nucleoside phosphorylase (EC 2.4.2.1) (PNP) from most bacteria (gene deoD). This enzyme catalyzes the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [1].
  • Uridine phosphorylase (EC 2.4.2.3) (UdRPase) from bacteria (gene udp) and mammals. Catalyzes the cleavage of uridine into uracil and ribose-1- phosphate. The products of the reaction are used either as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis [2].
  • 5'-methylthioadenosine phosphorylase (EC 2.4.2.28) (MTA phosphorylase) from Sulfolobus solfataricus [3].

As a signature pattern, we selected a conserved region in the central part of these enzymes.

Note:

It should be noted that mammalian and some bacterial PNP as well as eukaryotic MTA phosphorylase belong to a different family of phosphorylases (see <PDOC00954>).

Last update:

December 2004 / Pattern and text revised.

Technical section

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

PNP_UDP_1, PS01232; Purine and other phosphorylases family 1 signature  (PATTERN)


References

1AuthorsTakehara M., Ling F., Izawa S., Inoue Y., Kimura A.
TitleMolecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp.
SourceBiosci. Biotechnol. Biochem. 59:1987-1990(1995).
PubMed ID8534998

2AuthorsWatanabe S.-I., Hino A., Wada K., Eliason J.F., Uchida T.
TitlePurification, cloning, and expression of murine uridine phosphorylase.
SourceJ. Biol. Chem. 270:12191-12196(1995).
PubMed ID7744869

3AuthorsCacciapuoti G., Porcelli M., Bertoldo C., De Rosa M., Zappia V.
TitlePurification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds.
SourceJ. Biol. Chem. 269:24762-24769(1994).
PubMed ID7929153



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