| Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for production of useful amino acids. | |
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MedLine Citation:
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PMID: 21821743 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We determined the enzymatic characteristics of an industrially important biocatalyst, α-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. |
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Authors:
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Makoto Hibi; Takashi Kawashima; Tomohiro Kodera; Sergey V Smirnov; Pavel M Sokolov; Masakazu Sugiyama; Sakayu Shimizu; Kenzo Yokozeki; Jun Ogawa |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2011-08-05 |
Journal Detail:
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Title: Applied and environmental microbiology Volume: 77 ISSN: 1098-5336 ISO Abbreviation: Appl. Environ. Microbiol. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-09-23 Completed Date: 2012-01-19 Revised Date: 2012-04-02 |
Medline Journal Info:
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Nlm Unique ID: 7605801 Medline TA: Appl Environ Microbiol Country: United States |
Other Details:
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Languages: eng Pagination: 6926-30 Citation Subset: IM |
Affiliation:
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Industrial Microbiology, Graduate School of Agriculture, Kyoto University, Kitashirakawa-oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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metabolism* Bacillus thuringiensis / enzymology*, metabolism* Dioxygenases / metabolism* Hydroxylation Ketoglutaric Acids / metabolism Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Ketoglutaric Acids; 328-50-7/alpha-ketoglutaric acid; EC 1.13.11.-/Dioxygenases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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