Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate in the cytoplasm (cSHMT, SHMT1) and mitochondria (mSHMT, SHMT2). cSHMT preferentially supplies one-carbon units for thymidylate biosynthesis, depletes methylenetetrahydrofolate pools for S-adenosylmethionine (SAM) synthesis by synthesizing serine, sequesters 5-methyltetrahydrofolate, and inhibits SAM synthesis.
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Protein Aliases: epididymis secretory sperm binding protein Li 51e; GLY A+; glycine auxotroph A, human complement for hamster; Glycine hydroxymethyltransferase; serine aldolase; serine hydroxymethylase; serine hydroxymethyltransferase 2 (mitochondrial); Serine hydroxymethyltransferase, mitochondrial; Serine methylase; SHMT; SHMT 2; threonine aldolase
Gene Aliases: 2700043D08Rik; AA408223; AA986903; GLYA; HEL-S-51e; SHMT; SHMT2