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4.3.1.27 |
Activity |
4.3.1.27 |
Description |
Threo-3-hydroxy-D-aspartate ammonia-lyase |
PDB |
4PB5; |
PLP Fold Type |
III |
PLP-dependent Domain |
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Number of sequences |
11 |
Sequences in seed alignment |
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Reference sequence |
B2DFG5 |
Domain interval |
15-366 |
Catalytic site |
46 K |
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References |
Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M.
(2015) Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate
Appl Microbiol Biotechnol 99 7137-50. Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M. (2013) Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23. Acta Crystallogr Sect F Struct Biol Cryst Commun 69 1131-4. Maeda T, Takeda Y, Murakami T, Yokota A, Wada M. (2010) Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartatedehydratase, from Delftia sp. HT23 J Biochem 148 705-12. Articles on 4.3.1.27 |
last changed |
2017/09/06 11:21 |
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