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4.3.1.16 |
Activity |
4.3.1.16 |
Description |
Threo-3-hydroxyaspartate ammonia-lyase |
Notes |
Includes validated sequences from bacteria (Pseudomonas) and yeast. Enzymes most similar to serine racemases (Family 5.1.1.18) and D-erythro-3-hydroxyaspartate deaminases (Family bhcb). |
PDB |
1V71; |
PLP Fold Type |
II |
PLP-dependent Domain |
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Number of sequences |
13 |
Sequences in seed alignment |
|
Reference sequence |
BAF48772 |
Domain interval |
16-305 |
Catalytic site |
53 K |
| |
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. Articles on 4.3.1.16 |
last changed |
2019/11/25 16:34 |
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