Aspartate ammonia-lyase
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| 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
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J3U and 1JSW.
References
- ^ 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.
