Phosphoglycerate dehydrogenase (PHGDH) is involved in the early steps of L-serine synthesis in animal cells.In addition to D-serine, which is a significant agonist of the N-methyl-D-aspartate (NMDA) receptor, L-serine is an essential amino acid because it functions as a precursor to many other essential metabolites. The de novo serine biosynthetic pathway's first and only rate-limiting enzyme, PHGDH, catalyzes the oxidation of 3-PG produced during glycolysis to 3-phosphohydroxypyruvate (3-PHP).In a family with congenital microcephaly, psychomotor retardation, and other symptoms, mutations in the PHGDH gene have been discovered. Overexpression-related increases in PGDH levels are linked to a variety of cancers. Extracellular L-serine cannot support tumor cell proliferation in culture because PGDH is necessary for this process. This has given rise to the theory that the pathway serves a purpose other than supplying L-serine that is connected to tumor growth.
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