Purine nucleosidase
| purine nucleosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Purine nucleosidase tetramer, Saccharolobus solfataricus | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.2.1 | ||||||||
| CAS no. | 9025-44-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a purine nucleosidase (EC 3.2.2.1) is an enzyme that catalyzes the chemical reaction
- a purine nucleoside + H2O D-ribose + a purine base
Thus, the two substrates of this enzyme are purine nucleoside and H2O, whereas its two products are D-ribose and purine base.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is purine-nucleoside ribohydrolase. Other names in common use include nucleosidase, purine beta-ribosidase, purine nucleoside hydrolase, purine ribonucleosidase, ribonucleoside hydrolase, nucleoside hydrolase, N-ribosyl purine ribohydrolase, nucleosidase g, N-D-ribosylpurine ribohydrolase, inosine-adenosine-guanosine preferring nucleoside hydrolase, purine-specific nucleoside N-ribohydrolase, IAG-nucleoside hydrolase, and IAG-NH. This enzyme participates in purine metabolism and nicotinate and nicotinamide metabolism.
Structural studies
[edit]As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1EZR, 1HOZ, 1HP0, 1KIC, 1KIE, 1MAS, 1R4F, 2C40, 2FF1, 2FF2, and 2MAS.
References
[edit]- HEPPEL LA, HILMOE RJ (1952). "[Phosphorolysis and hydrolysis of purine ribosides by enzymes from yeast.]". J. Biol. Chem. 198 (2): 683–94. doi:10.1016/S0021-9258(18)55525-3. PMID 12999785.
- Kalckar HM. "Biosynthetic aspects of nucleosides and nucleic acids". Pubbl. Staz. Zool. Napoli: 87–103.
- Takagi Y, Horecker BL (1956). "Purification and properties of a bacterial riboside hydrolyase". J. Biol. Chem. 225 (1): 77–86. doi:10.1016/S0021-9258(18)64911-7. PMID 13416219.
- Tarr HLA (1955). "Fish muscle riboside hydrolases". Biochem. J. 59 (3): 386–391. doi:10.1042/bj0590386. PMC 1216255. PMID 14363106.
- Parkin DW (1996). "Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism". J. Biol. Chem. 271 (36): 21713–9. doi:10.1074/jbc.271.36.21713. PMID 8702965.
- S; Takeda, S; Xie, SX; Hatanaka, H; Ashikari, T; Amachi, T; Shimizu, S (2001). "Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi". Appl. Environ. Microbiol. 67 (4): 1783–7. doi:10.1128/AEM.67.4.1783-1787.2001. PMC 92797. PMID 11282633.
- Versees W, Decanniere K, Van Holsbeke E, Devroede N, Steyaert J (2002). "Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax". J. Biol. Chem. 277 (18): 15938–46. doi:10.1074/jbc.M111735200. PMID 11854281.
- Mazumder-Shivakumar D, Bruice TC (2005). "Computational study of IAG-nucleoside hydrolase: determination of the preferred ground state conformation and the role of active site residues". Biochemistry. 44 (21): 7805–17. doi:10.1021/bi047394h. PMID 15909995.
