Serine dehydratase (SDS)

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme primarily expressed in the liver, where it catalyzes the deamination of L-serine (and L-threonine) to produce pyruvate (or 2-oxobutyrate) and ammonia[3][5][11]. It is essential for gluconeogenesis from amino acids and thus plays a key role in maintaining glucose homeostasis. Structurally, human serine dehydratase is a homodimer comprised of two domains within each monomer—a large PLP-binding catalytic domain and a small regulatory domain—forming the active site at their interface[3][5]. The enzyme is found in various organisms and its structural properties vary among species, but its catalytic role in amino acid metabolism is highly conserved. Deficient activity of serine dehydratase can contribute to disease states associated with impaired serine and glycine metabolism, and the enzyme attracts interest in metabolic and neurodegenerative disease research. No clinically approved drugs are known to target serine dehydratase directly at this time.

Other names

L-serine dehydrataseL-threonine deaminaseSDHhSDHhepatic serine dehydrataseL-serine deaminaseL-threonine dehydrataseL-serine ammonia-lyaseTDH

Not applicable (no drugs targeting this enzyme are clinically established); enzyme catalyzes the PLP-dependent deamination of L-serine to pyruvate and ammonia[3][5][11]