Methylthioadenosine nucleosidase
methylthioadenosine nucleosidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.2.2.16 | ||||||||
CAS no. | 50812-28-7 | ||||||||
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 | ||||||||
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In enzymology, a methylthioadenosine nucleosidase (EC 3.2.2.16) is an enzyme that catalyzes the chemical reaction
- S-methyl-5'-thioadenosine + H2O S-methyl-5-thio-D-ribose + adenine
Thus, the two substrates of this enzyme are S-methyl-5'-thioadenosine and H2O, whereas its two products are S-methyl-5-thio-D-ribose and adenine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is S-methyl-5'-thioadenosine adeninehyrolase. Other names in common use include 5'-methylthioadenosine nucleosidase, MTA nucleosidase, MeSAdo nucleosidase, and methylthioadenosine methylthioribohydrolase. This enzyme participates in urea cycle and metabolism of amino groups and methionine metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1NC1, 1NC3, 1Y6Q, 1Y6R, 1ZOS, and 2H8G.
References
- Guranowski AB, Chiang PK, Cantoni GL (1981). "5'-Methylthioadenosine nucleosidase. Purification and characterization of the enzyme from Lupinus luteus seeds". Eur. J. Biochem. 114 (2): 293–9. doi:10.1111/j.1432-1033.1981.tb05148.x. PMID 6783408.
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