InterPro domain: IPR000845

Phosphorylases with this domain include:

• Purine nucleoside phosphorylase ( 2.4.2.1 ) (PNP) from most bacteria (gene deoD), which catalyses the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [ 1 ].
• Uridine phosphorylase ( 2.4.2.3 ) (UdRPase) from bacteria (gene udp) and mammals, which catalyses 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 ( 2.4.2.28 ) (MTA phosphorylase) from Sulfolobus solfataricus [ 3 ].
• Purine nucleoside phosphorylase ( 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 [ 4 ].
• 5'-methylthioadenosine phosphorylase ( 2.4.2.28 ) (MTA phosphorylase) from eukaryotes [ 5 ].

1. Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp. Biosci. Biotechnol. Biochem. 59, 1987-90
2. Purification, cloning, and expression of murine uridine phosphorylase. J. Biol. Chem. 270, 12191-6
3. 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. J. Biol. Chem. 269, 24762-9
4. Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J. Biol. Chem. 265, 1812-20
5. Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. Biochem. Biophys. Res. Commun. 223, 514-9