L-serine ammonia-lyase

The enzyme  L -serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction


 * L -serine = pyruvate + NH3 (overall reaction)
 * (1a) L -serine = 2-aminoprop-2-enoate + H2O
 * (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
 * (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)

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 (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase,  L -serine deaminase,  L -serine dehydratase, and  L -serine hydro-lyase (deaminating). This enzyme participates in glycine, serine, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes, , , and.