Serine hydroxymethyltransferase
（重定向自Glycine hydroxymethyltransferase）
![](/Images/godic/202501/15/EcSHMTPyMol5146.png")
![Glycine is formed Schiff base linked to the PLP in this mechanism, and the Schiff base linkage can hydrolyze to give the original PLP cofactor.](/Images/godic/202501/15/SHMT_Mechanism5146.jpg")
Serine hydroxymethyltransferase (SHMT) is a PLP dependent enzyme (EC2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF)to 5,10-methylenetetrahydrofolate. This reaction provides the largest part of the one-carbon units available to the cell.