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Hokkaido University Collection of Scholarly and Academic Papers >
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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
| 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)
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Submitter: 和田 大
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