Serine Dehydratase (SDS)

Serine dehydratase catalyzes the PLP-dependent alpha,beta-elimination of L-serine to pyruvate and ammonia. In mammals, SDH is found predominantly in the liver. Ogawa et al. (1989) cloned and sequenced human liver serine dehydratase and compared it with the enzyme in the rat.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine ammonia-lyase. Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, and L-serine hydro-lyase. This enzyme participates in glycine, serine and threonine metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.