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4.3.1.16 |
| Description |
Threo-3-hydroxyaspartate ammonia-lyase |
| Alternative names |
L-Threo-3-hydroxyaspartate dehydratase;
L-threo-3-hydroxyaspartate dehydratase. |
| Catalyzed reaction |
Threo-3-hydroxy-L-aspartate = oxaloacetate + NH(3) |
| Cofactor |
Pyridoxal-phosphate |
| Comments |
-The enzyme 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 and EC 4.3.1.27.
-Requires a divalent cation such as Mn(2+), Mg(2+), or Ca(2+).
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The enzyme from the bacterium Pseudomonas sp. T62 is highly specific, and does not accept any other stereoisomer of 3-hydroxyaspartate. In contrast, the homologous enzyme from Pseudomonas sp. N99 also efficiently degrades its enantiomer, D-erythro-3-hydroxyaspartate. |
| PDB |
1V71; |
| Organisms |
-Eubacteria -Fungi |
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Family |
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| Links |
Enzyme (activities) 4.3.1.16
BRENDA (activities) 4.3.1.16
KEGG (pathways) 4.3.1.16
PLPMDB (PLP mutants) 4.3.1.16
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| References |
Nagano, H.; Shibano, K.; Matsumoto, Y.; Yokota, A.; Wada, M.
(2017) Isolation and amino acid sequence of a dehydratase acting on d-erythro-3-hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate Biosci Biotechnol Biochem 81 1156-1164. Wada, M.; Nakamori, S.; Takagi, H.
(2003) Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity FEMS Microbiol Lett 225 189-93. Wada, M.; Matsumoto, T.; Nakamori, S.; Sakamoto, M.; Kataoka, M.; Liu, J. Q.; Itoh, N.; Yamada, H.; Shimizu, S. (1999) Purification and characterization of a novel enzyme, L-threo-3- hydroxyaspartate dehydratase, from Pseudomonas sp. T62 FEMS Microbiol Lett 179 147-51. |
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| last changed |
2019/06/20 13:41 |
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