2011年10月
Characterization of Bacillus thuringiensis L-Isoleucine Dioxygenase for Production of Useful Amino Acids
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
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- 巻
- 77
- 号
- 19
- 開始ページ
- 6926
- 終了ページ
- 6930
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1128/AEM.05035-11
- 出版者・発行元
- AMER SOC MICROBIOLOGY
We determined the enzymatic characteristics of an industrially important biocatalyst, alpha-ketoglutarate-dependent L-isoleucine dioxygenase (IDO), which was found to be the enzyme responsible for the generation of (2S,3R,4S)-4-hydroxyisoleucine in Bacillus thuringiensis 2e2. Depending on the amino acid used as the substrate, IDO catalyzed three different types of oxidation reactions: hydroxylation, dehydrogenation, and sulfoxidation. IDO stereoselectively hydroxylated several hydrophobic aliphatic L-amino acids, as well as L-isoleucine, and produced (S)-3-hydroxy-L-allo-isoleucine, 4-hydroxy-L-leucine, (S)-4-hydroxy-L-norvaline, 4-hydroxy-L-norleucine, and 5-hydroxy-L-norleucine. The IDO reaction product of L-isoleucine, (2S,3R,4S)-4-hydroxyisoleucine, was again reacted with IDO and dehydrogenated into (2S,3R)-2-amino-3-methyl-4-ketopentanoate, which is also a metabolite found in B. thuringiensis 2e2. Interestingly, IDO catalyzed the sulfoxidation of some sulfur-containing L-amino acids and generated L-methionine sulfoxide and L-ethionine sulfoxide. Consequently, the effective production of various modified amino acids would be possible using IDO as the biocatalyst.
- リンク情報
- ID情報
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- DOI : 10.1128/AEM.05035-11
- ISSN : 0099-2240
- PubMed ID : 21821743
- Web of Science ID : WOS:000295123300024