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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

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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 Browse this author
Shibano, Kana Browse this author
Matsumoto, Yu Browse this author
Yokota, Atsushi Browse this author →KAKEN DB
Wada, Masaru Browse this author →KAKEN DB
Keywords: 3-hydroxyaspartate
ammonia-lyase
enzymatic resolution
pyridoxal 5'-phosphate
Pseudomonas sp.N99
Issue Date: Jun-2017
Publisher: Taylor & Francis
Journal Title: Bioscience biotechnology and biochemistry
Volume: 81
Issue: 6
Start Page: 1156
End Page: 1164
Publisher DOI: 10.1080/09168451.2017.1295804
PMID: 28290777
Abstract: An enzyme catalyzing the ammonia-lyase reaction for the conversion of d-erythro-3-hydroxyaspartate to oxaloacetate was purified from the cell-free extract of a soil-isolated bacterium Pseudomonas sp. N99. The enzyme exhibited ammonia-lyase activity toward l-threo-3-hydroxyaspartate and d-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 of l-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) from Pseudomonas sp. T62 (74%) and Saccharomyces cerevisiae (64%) and serine racemase from Schizosaccharomyces pombe (65%). These results suggest that the enzyme is similar to l-threo-3-hydroxyaspartate ammonia-lyase from Pseudomonas sp. T62, which does not act on d-erythro-3-hydroxyaspartate. We also then used the recombinant enzyme expressed in Escherichia coli to produce optically pure l-erythro-3-hydroxyaspartate and d-threo-3-hydroxyaspartate from the corresponding dl-racemic mixtures. The enzymatic resolution reported here is one of the simplest and the first enzymatic method that can be used for obtaining optically pure l-erythro-3-hydroxyaspartate.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry on June 2017, available online: http://www.tandfonline.com/10.1080/09168451.2017.1295804
Type: article (author version)
URI: http://hdl.handle.net/2115/70654
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 和田 大

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