Threo-3-hydroxyaspartate ammonia-lyase
| threo-3-hydroxyaspartate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.16 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction
- threo-3-hydroxy-L-aspartate oxaloacetate + NH3
Hence, this enzyme has one substrate, threo-3-hydroxy-L-aspartate, and two products, oxaloacetate and NH3.
Nomenclature
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use include threo-3-hydroxyaspartate dehydratase, L-threo-3-hydroxyaspartate dehydratase, and threo-3-hydroxy-L-aspartate ammonia-lyase.
References
- Wada M, Matsumoto T, Nakamori S, Sakamoto M, Kataoka M, Liu JQ, Itoh N, Yamada H, Shimizu S (October 1999). "Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62". FEMS Microbiology Letters. 179 (1): 147–51. doi:10.1016/s0378-1097(99)00405-x. PMID 10481099.
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