L-serine ammonia-lyase

In enzymology, a L-serine ammonia-lyase is an enzyme that catalyzes the chemical reaction


 * L-serine $$\rightleftharpoons$$ pyruvate + NH3

Hence, this enzyme has one substrate, L-serine, and two products, pyruvate and NH3.

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 and threonine metabolism 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.