Open AccessCharacterization of Bacillus thuringiensis l -Isoleucine Dioxygenase for Production of Useful Amino Acids
Author(s) -
Makoto Hibi,
Takayuki Kawashima,
Tomohiro Kodera,
Sergey V. Smirnov,
Pavel M. Sokolov,
Masakazu Sugiyama,
Sakayu Shimizu,
Kenzo Yokozeki,
Jun Ogawa
Publication year - 2011
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.05035-11
Subject(s) - bacillus thuringiensis , isoleucine , dioxygenase , bacillaceae , bacillales , bacteria , amino acid , biology , bacillus (shape) , chemistry , biochemistry , microbiology and biotechnology , bacillus subtilis , leucine , enzyme , genetics
We determined the enzymatic characteristics of an industrially important biocatalyst, α-ketoglutarate-dependentl -isoleucine dioxygenase (IDO), which was found to be the enzyme responsible for the generation of (2S ,3R ,4S )-4-hydroxyisoleucine inBacillus 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 aliphaticl -amino acids, as well asl -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 ofl -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 inB. thuringiensis 2e2. Interestingly, IDO catalyzed the sulfoxidation of some sulfur-containingl -amino acids and generatedl -methionine sulfoxide andl -ethionine sulfoxide. Consequently, the effective production of various modified amino acids would be possible using IDO as the biocatalyst.