Serine dehydratase-like (SDSL)

Serine dehydratase-like (SDSL) is a human enzyme encoded by the SDSL gene, closely related to serine dehydratase (SDH) enzymes. It catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-serine to pyruvate and ammonia and can also act on L-threonine and L-/D-glutamate[2][5]. SDSL plays an important role in amino acid catabolism, particularly in gluconeogenesis and amino acid metabolism pathways. The enzyme is a member of the β-family of PLP-dependent lyases and contains a PALP domain[2][5]. SDSL is implicated in cancer biology, as alterations in its activity or expression are observed in tumorous tissues, and may also influence metabolic disorders associated with amino acid imbalance[1][2]. Its main known physiological cofactor is pyridoxal phosphate. Known inhibitors include several amino acids and metabolic intermediates, and the enzyme is subject to hormonal regulation in the liver[1]. Little is known about human SDSL function specifically due to low enzymatic activity in the human liver; its best-studied function is in model organisms and metabolic studies.

Other names

Cancerous serine dehydratasecSDHGlutamate racemaseL-serine deaminaseL-serine dehydratase/L-threonine deaminaseL-threonine dehydrataseSerine dehydratase 2SDH 2SDHLSDS-RS1TDH

Dehydrative deamination (PLP-dependent catalysis), Competitive inhibition (by L-cysteine, D-serine, L-threonine), Noncompetitive inhibition (by homocysteine), Regulation by hormonal signals (insulin/epinephrine inhibit, glucagon upregulates)