Serine biosynthesis (Saccharomyces cerevisiae)

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L-serine biosynthesis is a major metabolic pathway in many organisms. Its end product, L-serine, is not only used in protein synthesis, but also as a precursor for the biosynthesis of glycine, cysteine, tryptophan, and phospholipids. In addition, it directly or indirectly serves as a source of one-carbon units for the biosynthesis of various compounds.

In the pathway described here, which operates in bacteria, yeast, some protists, plant plastids and animals, serine is derived from 3-phospho-D-glycerate, an intermediate of glycolysis.

Regulation of the pathway is mainly accomplished by feedback inhibition of the enzyme that catalyzes the first committed step, SER3/SER33, phosphoglycerate dehydrogenase. The second enzyme in the pathway, SER1, phosphoserine transaminase, requires pyridoxal 5'-phosphate (PLP) as a cofactor and is also required for the biosynthesis of PLP itself. Thus the cell must ensure that the supply of PLP is adequate. Little biochemical work has been done on the final enzyme of the pathway, SER2, phosphoserine phosphatase.

Description from https://pathway.yeastgenome.org/.