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 | ||||||||
| |||||||||
The enzyme aspartate 1-decarboxylase (EC 4.1.1.11) 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[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.
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.
