| Structural highlights
Function
IDO_BACTU Catalyzes the hydroxylation of L-isoleucine to produce (4S)-4-hydroxy-L-isoleucine (PubMed:20665018, PubMed:19850012, PubMed:21821743). Can also catalyze the hydroxylation of L-leucine, L-norvaline, L-norleucine and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine (PubMed:21821743).[1] [2] [3]
References
- ↑ Kodera T, Smirnov SV, Samsonova NN, Kozlov YI, Koyama R, Hibi M, Ogawa J, Yokozeki K, Shimizu S. A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine. Biochem Biophys Res Commun. 2009 Dec 18;390(3):506-10. PMID:19850012 doi:10.1016/j.bbrc.2009.09.126
- ↑ Smirnov SV, Kodera T, Samsonova NN, Kotlyarova VA, Rushkevich NY, Kivero AD, Sokolov PM, Hibi M, Ogawa J, Shimizu S. Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-hydroxyisoleucine. Appl Microbiol Biotechnol. 2010 Oct;88(3):719-26. PMID:20665018 doi:10.1007/s00253-010-2772-3
- ↑ Hibi M, Kawashima T, Kodera T, Smirnov SV, Sokolov PM, Sugiyama M, Shimizu S, Yokozeki K, Ogawa J. Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for production of useful amino acids. Appl Environ Microbiol. 2011 Oct;77(19):6926-30. PMID:21821743 doi:10.1128/AEM.05035-11
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