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- Title
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.
- Authors
Nagano, Hiroyuki; Shibano, Kana; Matsumoto, Yu; Yokota, Atsushi; Wada, Masaru
- Abstract
An enzyme catalyzing the ammonia-lyase reaction for the conversion ofd-erythro-3-hydroxyaspartate to oxaloacetate was purified from the cell-free extract of a soil-isolated bacteriumPseudomonassp. N99. The enzyme exhibited ammonia-lyase activity towardl-threo-3-hydroxyaspartate andd-erythro-3-hydroxyaspartate, but not toward other 3-hydroxyaspartate isomers. The deduced amino acid sequence of the enzyme, which belongs to the serine/threonine dehydratase family, shows similarity to the sequence ofl-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) fromPseudomonassp. T62 (74%) andSaccharomyces cerevisiae(64%) and serine racemase fromSchizosaccharomyces pombe(65%). These results suggest that the enzyme is similar tol-threo-3-hydroxyaspartate ammonia-lyase fromPseudomonassp. T62, which does not act ond-erythro-3-hydroxyaspartate. We also then used the recombinant enzyme expressed inEscherichia colito produce optically purel-erythro-3-hydroxyaspartate andd-threo-3-hydroxyaspartate from the correspondingdl-racemic mixtures. The enzymatic resolution reported here is one of the simplest and the first enzymatic method that can be used for obtaining optically purel-erythro-3-hydroxyaspartate. A novel enzyme “d-erythro-3-hydroxyaspartate dehydratase” was applied to optically activel-erythro-3-hydroxyaspartate production.
- Subjects
PSEUDOMONAS; ASPARTATES; AMINO acid sequence
- Publication
Bioscience, Biotechnology & Biochemistry, 2017, Vol 81, Issue 6, p1156
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1080/09168451.2017.1295804