PROSITE documentation PDOC00946Purine 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.
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Technical section
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References
| 1 | Authors | Takehara M. Ling F. Izawa S. Inoue Y. Kimura A. |
| Title | Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp. | |
| Source | Biosci. Biotechnol. Biochem. 59:1987-1990(1995). | |
| PubMed ID | 8534998 |
| 2 | Authors | Watanabe S.-I. Hino A. Wada K. Eliason J.F. Uchida T. |
| Title | Purification, cloning, and expression of murine uridine phosphorylase. | |
| Source | J. Biol. Chem. 270:12191-12196(1995). | |
| PubMed ID | 7744869 |
| 3 | Authors | Cacciapuoti G. Porcelli M. Bertoldo C. De Rosa M. Zappia V. |
| Title | Purification 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. | |
| Source | J. Biol. Chem. 269:24762-24769(1994). | |
| PubMed ID | 7929153 |
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