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 studiesedit
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.
Referencesedit
HEPPEL LA, HILMOE RJ (1952). "[Phosphorolysis and hydrolysis of purine ribosides by enzymes from yeast.]". J. Biol. Chem. 198 (2): 683–94. 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. PMID 13416219.
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. PMC92797. 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.
purine, nucleosidase, enzymology, purine, nucleosidase, enzyme, that, catalyzes, chemical, reactionpurine, nucleosidase, tetramer, saccharolobus, solfataricusidentifiersec, 1cas, 9025, 9databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg. In enzymology a purine nucleosidase EC 3 2 2 1 is an enzyme that catalyzes the chemical reactionpurine nucleosidasePurine nucleosidase tetramer Saccharolobus solfataricusIdentifiersEC no 3 2 2 1CAS no 9025 44 9DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins a purine nucleoside H2O displaystyle rightleftharpoons D ribose a purine baseThus 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 editAs 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 editHEPPEL LA HILMOE RJ 1952 Phosphorolysis and hydrolysis of purine ribosides by enzymes from yeast J Biol Chem 198 2 683 94 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 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 Portal nbsp Biology This EC 3 2 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Purine nucleosidase amp oldid 1172359006, wikipedia, wiki, book, books, library,
