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Article

A novel tumor suppressor function of glycine N-methyltransferase is independent of its catalytic activity but requires nuclear localization.

PloS one - 1 Jan 2013

DebRoy Suchandra, Kramarenko Inga I, Ghose Sampa, Oleinik Natalia V, Krupenko Sergey A, Krupenko Natalia I

Abstract excerpt

Glycine N-methyltransferase (GNMT), an abundant cytosolic enzyme, catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine generating S-adenosylhomocysteine and sarcosine (N-methylglycine). This reaction is regulated by 5-methyltetrahydrofolate, which inhibits the enzyme catalysis. In the present study, we observed that GNMT is strongly down regulated in human cancers and is...

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Source

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Identifiers

PMID: 23936142
DOI: 10.1371/journal.pone.0070062
PMCID: PMC3728347

Genes

GNMT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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