Glycine hydroxymethyltransferase

In enzymology, a glycine hydroxymethyltransferase is an enzyme that catalyzes the chemical reaction


 * 5,10-methylenetetrahydrofolate + glycine + H2O $$\rightleftharpoons$$ tetrahydrofolate + L-serine

The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, glycine, and H2O, whereas its two products are tetrahydrofolate and L-serine.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase. Other names in common use include serine aldolase, threonine aldolase, serine hydroxymethylase, serine hydroxymethyltransferase, allothreonine aldolase, L-serine hydroxymethyltransferase, L-threonine aldolase, serine hydroxymethyltransferase, and serine transhydroxymethylase. This enzyme participates in 5 metabolic pathways: glycine, serine and threonine metabolism, lysine degradation, cyanoamino acid metabolism, one carbon pool by folate, and methane metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , , , , , and.