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 and H2O, whereas its two products are 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.
- EC 3.2.2
- Enzymes of known structure
- EC 3.2 stubs