Erythro-3-hydroxyaspartate ammonia-lyase
| erythro-3-hydroxyaspartate ammonia-lyase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 4.3.1.20 | ||||||
| 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 / EGO | ||||||
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In enzymology, an erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) is an enzyme that catalyzes the chemical reaction
- erythro-3-hydroxy-Ls-aspartate
oxaloacetate + NH3
Hence, this enzyme has one substrate, erythro-3-hydroxy-Ls-aspartate, and two products, oxaloacetate and NH3.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is erythro-3-hydroxy-Ls-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use include 3-hydroxyaspartate dehydratase, erythro-beta-hydroxyaspartate dehydratase, erythro-3-hydroxyaspartate dehydratase, erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating), and erythro-3-hydroxy-Ls-aspartate ammonia-lyase. It employs one cofactor, pyridoxal phosphate.
[edit] References
- Gibbs RG, Morris JG (1965). "Purification and properties of erythro-beta-hydroxyasparate dehydratase from Micrococcus denitrificans". Biochem. J. 97 (2): 547–54. PMC 1264673. PMID 16749162. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1264673.
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oxaloacetate + NH3