Aspartate 1-decarboxylase

aspartate 1-decarboxylase
aspartate 1-decarboxylase heterooctamer, E.Coli
Identifiers
EC no.	4.1.1.11
CAS no.	9024-58-2
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 enzyme aspartate 1-decarboxylase (EC 4.1.1.11) catalyzes the chemical reaction

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

Hence, this enzyme has one substrate, L-aspartate, and two products, beta-alanine and CO₂.

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 1-carboxy-lyase (beta-alanine-forming). Other names in common use include aspartate alpha-decarboxylase, L-aspartate alpha-decarboxylase, aspartic alpha-decarboxylase, and L-aspartate 1-carboxy-lyase. This enzyme participates in alanine and aspartate metabolism and beta-alanine metabolism.

As of late 2007^[update], 12 structures have been solved for this class of enzymes, with PDB accession codes 1AW8, 1PPY, 1PQE, 1PQF, 1PQH, 1PT0, 1PT1, 1PYQ, 1PYU, 1UHD, 1UHE, and 2C45.

• Williamson JM, Brown GM (1979). "Purification and properties of L-Aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli". J. Biol. Chem. 254 (16): 8074–82. PMID 381298.