Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes.

[citation needed] Serine Dehydratase is also known as:[2] The holoenzyme SDH contains 319 residues, one PLP cofactor molecule.

A Schiff base linkage is made and the aminoacrylate group is released which undergoes non-enzymatic hydrolytic deamination to pyruvate.

[4] According to the series of assays performed by Cleland (1967), the linear rate of pyruvate formation at various concentrations of inhibitors demonstrated that L-cysteine and D-serine competitively inhibit the enzyme SDH.

Moreover, insulin is known to accelerate glycolysis and repress induction of liver serine dehydratase in adult diabetic rats.

[7] Studies have been conducted to show insulin causes a 40-50% inhibition of the induction serine dehydratase by glucagon in hepatocytes of rats.

And glucagon gives the signal to repress gluconeogenesis and increase the amount of free glucose in the blood by releasing glycogen stores from the liver.

The observed enzyme imbalance in these tumors shows that an increased capacity for the synthesis of serine is coupled to its utilization for nucleotide biosynthesis as a part of the commitment to cellular replication in cancer cells.

[15] Human and rat serine dehydratase cDNA are identical except for a 36 amino acid residue stretch.