Aspartate ammonia-lyase

The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction

L-aspartate ${\displaystyle \rightleftharpoons }$ fumarate + NH₃

aspartate ammonia-lyase
Aspartate ammonia-lyase homotetramer, Bacillus sp. YM55-1
Identifiers
EC no.	4.3.1.1
CAS no.	9027-30-9
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

The reaction is the basis of the industrial synthesis of aspartate.^[1]

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-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J3U and 1JSW.