Purine nucleosidase explained
purine nucleosidase |
Ec Number: | 3.2.2.1 |
Cas Number: | 9025-44-9 |
Go Code: | 0008477 |
Width: | 270 |
In enzymology, a purine nucleosidase 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
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,,,,, and .
References
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- Tarr HLA . 1955 . Fish muscle riboside hydrolases . Biochem. J. . 59 . 3 . 386 - 391 . 10.1042/bj0590386 . 14363106 . 1216255 .
- Parkin DW . 1996 . Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism . J. Biol. Chem. . 271 . 21713 - 9 . 8702965 . 36 . 10.1074/jbc.271.36.21713. free .
- S . 2001 . Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi . Appl. Environ. Microbiol. . 67 . 1783 - 7 . 11282633 . 10.1128/AEM.67.4.1783-1787.2001 . Takeda . S . Xie . SX . Hatanaka . H . Ashikari . T . Amachi . T . Shimizu . S . 4 . 92797 .
- 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 . 15938 - 46 . 11854281 . 10.1074/jbc.M111735200 . 18 . free .
- 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 . 7805 - 17 . 15909995 . 10.1021/bi047394h . 21 .