PROSITE documentation PDOC00090
Serine hydroxymethyltransferase pyridoxal-phosphate attachment site


Serine hydroxymethyltransferase (EC (SHMT) [1] catalyzes the transfer of the hydroxymethyl group of serine to tetrahydrofolate to form 5,10-methylenetetrahydrofolate and glycine. In vertebrates, it exists in a cytoplasmic and a mitochondrial form whereas only one form is found in prokaryotes. Serine hydroxymethyltransferase is a pyridoxal-phosphate containing enzyme. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme.

Last update:

April 2006 / Pattern revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

SHMT, PS00096; Serine hydroxymethyltransferase pyridoxal-phosphate attachment site  (PATTERN)


1AuthorsUsha R. Savithri H.S. Rao N.A.
TitleThe primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases.
SourceBiochim. Biophys. Acta 1204:75-83(1994).
PubMed ID8305478

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