| EC |
4.3.1.20 |
| Accepted name: |
erythro-3-hydroxy-L-aspartate ammonia-lyase |
| Reaction: |
erythro-3-hydroxy-L-aspartate = oxaloacetate + NH3 |
| Other name(s): |
erythro-β-hydroxyaspartate dehydratase; erythro-3-hydroxyaspartate dehydratase; erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating); erythro-3-hydroxy-Ls-aspartate ammonia-lyase |
| Systematic name: |
erythro-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming) |
| Comments: |
A pyridoxal-phosphate protein. The enzyme, which was characterized from the bacterium Paracoccus denitrificans NCIMB 8944, is highly specific for the L-isomer of erythro-3-hydroxyaspartate. Different from EC 4.3.1.16, threo-3-hydroxy-L-aspartate ammonia-lyase and EC 4.3.1.27, threo-3-hydroxy-D-aspartate ammonia-lyase. Requires a divalent cation such as Mn2+, Mg2+, and Ca2+. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-74-7 |
| References: |
| 1. |
Gibbs, R.G. and Morris, J.G. Purification and properties of erythro-β-hydroxyaspartate dehydratase from Micrococcus denitrificans. Biochem. J. 97 (1965) 547–554. [PMID: 16749162] |
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| [EC 4.3.1.20 created 1972 as EC 4.2.1.38, transferred 2001 to EC 4.3.1.20, modified 2011] |
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