|
type |
Journal Article |
authors |
Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M. |
title |
Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23. |
journal |
Acta Crystallogr Sect F Struct Biol Cryst Commun |
Activity |
4.3.1.27 |
Family |
4.3.1.27 |
sel |
selected |
ui |
24100565 |
year |
(2013) |
volume |
69 |
number |
10 |
pages |
1131-4 |
| |
abstract |
D-threo-3-Hydroxyaspartate dehydratase (D-THA DH) isolated from the soil bacterium Delftia sp. HT23 is a novel enzyme consisting of 380 amino-acid residues which catalyzes the conversion of D-threo-3-hydroxyaspartate to oxaloacetate and ammonia. D-THA DH also catalyzes the dehydration of L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate and D-serine. The amino-acid sequence of D-THA DH shows significant similarity to that of two eukaryotic D-serine dehydratases derived from Saccharomyces cerevisiae and chicken kidney. D-THA DH is classified into the fold-type III group of pyridoxal enzymes and is the first example of a fold-type III dehydratase derived from a prokaryote. Overexpression of recombinant D-THA DH was carried out using a Rhodococcus erythropolis expression system and the obtained protein was subsequently purified and crystallized. The crystals of D-THA DH belonged to space group I4₁22, with unit-cell parameters a=b=157.3, c=157.9 Å. Single-wavelength anomalous diffraction data were collected to a resolution of 2.0 Å using synchrotron radiation at the wavelength of the Br K absorption edge. |
last changed |
2014/02/24 11:05 |
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