FUNCTION Catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed:23438750, PubMed:3029074, PubMed:9305964). Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (PubMed:9305964).CATALYTIC ACTIVITY inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthineCATALYTIC ACTIVITY guanosine + phosphate = alpha-D-ribose 1-phosphate + guanineCATALYTIC ACTIVITY 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanineCATALYTIC ACTIVITY 2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + hypoxanthineACTIVITY REGULATION Inhibited by 5'-deaza-1'-aza-2c-deoxy-1'-(9-methylene)-Immucilin-G (DADMe-ImmG).BIOPHYSICOCHEMICAL PROPERTIES kcat is 57 sec(-1) with inosine as substrate (PubMed:9305964). kcat is 47 sec(-1) with inosine as substrate (PubMed:23438750). kcat is 70 sec(-1) with hypoxanthine as substrate (PubMed:9305964). kcat is 28 sec(-1) with guanosine as substrate (PubMed:9305964). kcat is 48 sec(-1) with guanine as substrate (PubMed:9305964). kcat is 0.0024 sec(-1) with adenosine as substrate (PubMed:9305964). kcat is 0.31 sec(-1) with adenine as substrate (PubMed:9305964).PATHWAY Purine metabolism; purine nucleoside salvage.SUBUNIT Homotrimer.INTERACTION Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the PNP/MTAP phosphorylase family.ONLINE INFORMATION NP mutation db
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