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Article

Structure-based mechanism for early PLP-mediated steps of rabbit cytosolic serine hydroxymethyltransferase reaction.

BioMed research international - 1 Jan 2013

Di Salvo Martino L, Scarsdale J Neel, Kazanina Galina, Contestabile Roberto, Schirch Verne, Wright H Tonie

Abstract excerpt

Serine hydroxymethyltransferase catalyzes the reversible interconversion of L-serine and glycine with transfer of one-carbon groups to and from tetrahydrofolate. Active site residue Thr254 is known to be involved in the transaldimination reaction, a crucial step in the catalytic mechanism of all pyridoxal 5'-phosphate- (PLP-) dependent enzymes, which determines binding of substrates and release of products. In...

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Identifiers

PMID: 23956983
DOI: 10.1155/2013/458571
PMCID: PMC3728543

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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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