Ribosylpyrimidine nucleosidase

In enzymology, a ribosylpyrimidine nucleosidase (EC 3.2.2.8) is an enzyme that catalyzes the chemical reaction

a pyrimidine nucleoside + H2O D-ribose + a pyrimidine base
ribosylpyrimidine nucleosidase
Identifiers
EC number3.2.2.8
CAS number37288-60-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are pyrimidine nucleoside and H2O, whereas its two products are D-ribose and pyrimidine 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 pyrimidine-nucleoside ribohydrolase. Other names in common use include N-ribosylpyrimidine nucleosidase, pyrimidine nucleosidase, N-ribosylpyrimidine ribohydrolase, pyrimidine nucleoside hydrolase, RihB, YeiK, and nucleoside ribohydrolase. This enzyme participates in purine metabolism and pyrimidine metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Q8F and 1YOE.

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References
    • Terada M, Tatibana M, Hayaishi O (1967). "Purification and properties of nucleoside hydrolase from Pseudomonas fluorescens". J. Biol. Chem. 242 (23): 5578–85. PMID 12325375.
    • Petersen C, Moller LB (2001). "The RihA, RihB, and RihC ribonucleoside hydrolases of Escherichia coli. Substrate specificity, gene expression, and regulation". J. Biol. Chem. 276 (2): 884–94. doi:10.1074/jbc.M008300200. PMID 11027694.
    • Giabbai B, Degano M (2004). "Cloning, purification, crystallization and X-ray analysis of the Escherichia coli pyrimidine nucleoside hydrolase YeiK". Acta Crystallogr. D. 60 (Pt 3): 524–7. doi:10.1107/S0907444903028488. PMID 14993681.
    • Giabbai B, Degano M (2004). "Crystal structure to 1.7 a of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy". Structure. 12 (5): 739–49. doi:10.1016/j.str.2004.03.018. PMID 15130467.


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