| EC |
4.3.1.16 |
| Accepted name: |
threo-3-hydroxy-L-aspartate ammonia-lyase |
| Reaction: |
threo-3-hydroxy-L-aspartate = oxaloacetate + NH3 |
| Other name(s): |
L-threo-3-hydroxyaspartate dehydratase; threo-3-hydroxyaspartate ammonia-lyase |
| Systematic name: |
threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming) |
| Comments: |
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Pseudomonas sp. T62, is highly specific, and does not accept any other stereoisomer of 3-hydroxyaspartate. Different from EC 4.3.1.20, erythro-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+, or Ca2+. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 248270-70-4 |
| References: |
| 1. |
Wada, M., Matsumoto, T., Nakamori, S., Sakamoto, M., Kataoka, M., Liu, J.-Q., Itoh, N., Yamada, H. and Shimizu, S. Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62. FEMS Microbiol. Lett. 179 (1999) 147–151. [DOI] [PMID: 10481099] |
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| [EC 4.3.1.16 created 2001, modified 2011] |
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