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Methylthioadenosine nucleosidase

class of enzymes

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionSep 11, 2026
Entity authorityQ6824058
Source-derived summary

Methylthioadenosine nucleosidase (EC 3.2.2.16) is an enzyme characterised from Lupinus luteus that catalyzes the hydrolysis of 5′-methylthioadenosine to S-methyl-5-thio-D-ribose and adenine.

The enzyme is widely present in plants, including rice and Arabidopsis thaliana. Inhibition of the enzyme has been studied as a way to control the bacterium Helicobacter pylori.

This enzyme is a hydrolase, specifically a glycosylase that hydrolyses 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.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1NC1​, PDB: 1NC3​, PDB: 1Y6Q​, PDB: 1Y6R​, PDB: 1ZOS​, and PDB: 2H8G​.

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The public source identifies “Methylthioadenosine nucleosidase” as class of enzymes. This brief keeps that definition visible, then builds a research path around Methylthioadenosine, nucleosidase and class.

Editorial reviewA dependable orientation record for establishing vocabulary, names and a first evidence trail. The current lead gives the account dated anchors—2007—that can be checked directly. The selected authority fields contribute no independent date. Its value is orientation rather than verdict, with Methylthioadenosine, nucleosidase and class providing the first useful test.
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This entry incorporates text from Methylthioadenosine nucleosidase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.