| EC |
4.3.1.27 |
| Accepted name: |
threo-3-hydroxy-D-aspartate ammonia-lyase |
| Reaction: |
threo-3-hydroxy-D-aspartate = oxaloacetate + NH3 |
| Other name(s): |
D-threo-3-hydroxyaspartate dehydratase |
| Systematic name: |
threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming) |
| Comments: |
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Delftia sp. HT23, also has activity against L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate, and D-serine. Different from EC 4.3.1.20, erythro-3-hydroxy-L-aspartate ammonia-lyase and EC 4.3.1.16, threo-3-hydroxy-L-aspartate ammonia-lyase. Requires a divalent cation such as Mn2+, Co2+ or Ni2+. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Maeda, T., Takeda, Y., Murakami, T., Yokota, A. and Wada, M. Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23. J. Biochem. 148 (2010) 705–712. [DOI] [PMID: 20843822] |
|
| [EC 4.3.1.27 created 2011] |
| |
|
| |
|