Aspartate ammonia-lyase
(Redirected from Aspartase)
| aspartate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Aspartate ammonia-lyase homotetramer, Bacillus sp. YM55-1 | |||||||||
| Identifiers | |||||||||
| EC no. | 4.3.1.1 | ||||||||
| CAS no. | 9027-30-9 | ||||||||
| 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 ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction
- L-aspartate fumarate + NH3
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.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J3U and 1JSW.
References
[edit]- ^ Karlheinz Drauz; Ian Grayson; Axel Kleemann; Hans-Peter Krimmer; Wolfgang Leuchtenberger; Christoph Weckbecker (2006). "Amino Acids". Ullmann's Encyclopedia of Industrial Chemistry. Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2. ISBN 978-3527306732.
- Ellfolk N, Kjærgård T, Bánhidi ZG, Virtanen AI, Sörensen NA (1953). "Studies on aspartase. 1. Quantitative separation of aspartase from bacterial cells, and its partial purification". Acta Chem. Scand. 7: 824–830. doi:10.3891/acta.chem.scand.07-0824.
