Erythro-3-hydroxyaspartate ammonia-lyase
From Wikipedia, the free encyclopedia
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
- IUBMB entry for 4.3.1.20
- BRENDA references for 4.3.1.20 (Recommended.)
- PubMed references for 4.3.1.20
- PubMed Central references for 4.3.1.20
- Google Scholar references for 4.3.1.20
- Gibbs RG, Morris JG (1965). "Purification and properties of erythro-beta-hydroxyasparate dehydratase from Micrococcus denitrificans". Biochem. J. 97: 547–54. PMID 16749162.

