Aspartate 1-decarboxylase

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aspartate 1-decarboxylase
4crz.jpg
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

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

L-aspartate 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.

Structural studies[edit]

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.

References[edit]

  • 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.