PROSITE documentation PDOC00954Purine and other phosphorylases family 2 signature
Description
The following phosphorylases belongs to the same family:
- Purine nucleoside phosphorylase (EC 2.4.2.1) (PNP) from mammals as well as from some bacteria (gene deoD). This enzyme catalyzes the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [1].
- 5'-methylthioadenosine phosphorylase (EC 2.4.2.28) (MTA phosphorylase) from eukaryotes [2].
- Xanthosine phosphorylase (EC 2.4.2.-) from Escherichia coli (gene xapA). This enzyme can degrade all purine nucleosides except adenosine and deoxyadenosine [3].
This family also includes the following uncharacterized proteins:
- Yeast hypothetical protein YLR017w.
- Fission yeast hypothetical protein SpAC16C9.02c.
- Methanococcus jannaschii hypothetical protein MJ0060.
- Rhodospirillum rubrum hypothetical protein in petC 3'region.
As a signature pattern, we selected a conserved region in the central part of these enzymes.
Note:It should be noted that most bacterial PNP as well as archaebacterial MTA phosphorylase belong to a different family of phosphorylases (see <PDOC00946>).
Last update:December 2004 / Pattern and text revised.
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Technical section
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References
1 | Authors | Ealick S.E. Rule S.A. Carter D.C. Greenhough T.J. Babu Y.S. Cook W.J. Habash J. Helliwell J.R. Stoeckler J.D. Parks R.E. Jr. Chen S.-F. Bugg C.E. |
Title | Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. | |
Source | J. Biol. Chem. 265:1812-1820(1990). | |
PubMed ID | 2104852 |
2 | Authors | Della Ragione F. Takabayashi K. Mastropietro S. Mercurio C. Oliva A. Russo G.L. Della Pietra V. Borriello A. Nobori T. Carson D.A. Zappia V. |
Title | Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. | |
Source | Biochem. Biophys. Res. Commun. 223:514-519(1996). | |
PubMed ID | 8687427 |
3 | Authors | Seeger C. Poulsen C. Dandanell G. |
Title | Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli. | |
Source | J. Bacteriol. 177:5506-5516(1995). | |
PubMed ID | 7559336 |
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