Aspartate ammonia-lyase
From Wikipedia, the free encyclopedia
The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction
- L-aspartate fumarate + NH3
| aspartate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Aspartate ammonia-lyase homotetramer, Bacillus sp. YM55-1 | |||||||||
| Identifiers | |||||||||
| EC no. | 4.3.1.1 | ||||||||
| CAS no. | 9027-30-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The reaction is the basis of the industrial synthesis of aspartate.[1]
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism.
