Aspartate 4-decarboxylase

In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction

L-aspartate ${\displaystyle \rightleftharpoons }$ L-alanine + CO₂

aspartate 4-decarboxylase
Aspartate beta-decarboxylase dodekamer, Comamonas testosteroni
Identifiers
EC no.	4.1.1.12
CAS no.	9024-57-1
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

Hence, this enzyme has one substrate, L-aspartate, and two products, L-alanine and CO₂. This reaction is the basis of the industrial synthesis of L-alanine.^[1]

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-aspartate 4-carboxy-lyase (L-alanine-forming). Other names in common use include desulfinase, aminomalonic decarboxylase, aspartate beta-decarboxylase, aspartate omega-decarboxylase, aspartic omega-decarboxylase, aspartic beta-decarboxylase, L-aspartate beta-decarboxylase, cysteine sulfinic desulfinase, L-cysteine sulfinate acid desulfinase, and L-aspartate 4-carboxy-lyase. This enzyme participates in alanine and aspartate metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.