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)

L-serine ammonia-lyase
Serine dehydratase monomer, Human
Identifiers
EC no.	4.3.1.17
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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 1P5J, 1PWE, 1PWH, and 2IQQ.