Aspartate 1-decarboxylase

In enzymology, an aspartate 1-decarboxylase (EC 4.1.1.11) is an enzyme that catalyzes the chemical reaction

L-aspartate beta-alanine + CO2
aspartate 1-decarboxylase
aspartate 1-decarboxylase heterooctamer, E.Coli
Identifiers
EC number4.1.1.11
CAS number9024-58-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

Structural studies

As of late 2007, 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.

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References
    • 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.


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