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B6db references: 24100565

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 . Single-wavelength anomalous diffraction data were collected to a resolution of 2.0  using synchrotron radiation at the wavelength of the Br K absorption edge.
last changed 2014/02/24 11:05

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