cSHMT 抗体 (S-W6): sc-100849

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. Sheep liver cytosolic recombinant SHMT (scSHMT) Lys-71, Arg-80 and Asp 89 residues influence intra-subunit ionic interactions essential for catalytic activity; Tyr 72, Asp 227 and His-356 residues in the active site interact with PLP and maintain the tetrameric structure. Human cSHMT and mSHMT genes map to 17p11.2 and 12q13, respectively. The cDNA for the mitochondrial enzyme encodes a mature protein of 474 residues.