Nonetheless, the phosphorylated pathway that PHGDH participates in is still suspected to have an essential role in serine synthesis used in the developmental signaling of plants.

[10] 3-phosphoglycerate dehydrogenase works via an induced fit mechanism to catalyze the transfer of a hydride from the substrate to NAD+, a required cofactor.

Given that PHGDH represents the committed step in the production of serine in the cell, flux through the pathway must be carefully controlled.

[12] The mechanism of inhibition is Vmax type, indicating that serine affects the reaction rate rather than the binding affinity of the active site.

At any time, only a maximum of two adjacent subunits present a catalytically active site; the other two are forced into an inactive conformation.

It is noted that the human enzyme more closely resembles that of M. tuberculosis, including the site for allosteric substrate inhibition.

[20] In addition significantly shortening lifespan, PHGDH deficiencies are known to cause congenital microcephaly, psychomotor retardation, and intractable seizures in both humans and rats, presumably due to the essential signaling within the nervous system that serine, glycine, and other downstream molecules are intimately involved with.

[23] This finding suggests that pathways providing an outlet for diverting carbon out of glycolysis may be beneficial for rapid cell growth.