Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-hydroxyisoleucine

Smirnov, Sergey V.; Kodera, Tomohiro; Samsonova, Natalya N.; Kotlyarova, Veronika A.; Rushkevich, Natalya Yu; Kivero, A. D.; Sokolov, Pavel M.; Hibi, Makoto; Ogawa, Jun; Shimizu, Sakayu

doi:10.1007/s00253-010-2772-3

Cited by 71 publications

(61 citation statements)

References 18 publications

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“…In our previous work, together with the aldolase-transaminase coupling reaction for HIL production from acetaldehyde, ␣-ketobutyrate, and L-glutamate (24,32), a highly efficient biotransformation system converting L-Ile into (2S,3R,4S)-HIL using IDO was developed (31). A genetically manipulated E. coli strain that accumulated ␣KG and was able to efficiently transport the branched-chain amino acid was used as the host strain in order to accelerate the hydroxylation reaction by heterologously expressed IDO.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of Bacillus thuringiensis l -Isoleucine Dioxygenase for Production of Useful Amino Acids

Hibi

Kawashima

Kodera

et al. 2011

Appl Environ Microbiol

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We determined the enzymatic characteristics of an industrially important biocatalyst, ␣-ketoglutaratedependent 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.Hydroxy amino acids are unusual hydroxylated amino acids and are ubiquitous in nature. They exist as secondary metabolites and components of peptides and proteins. Free amino acids are mostly found in higher plants (3,29), and also, free threo-3-hydroxy-L-asparagine has been found in human urine (25) and free 3-hydroxy-

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Section: Discussionmentioning

confidence: 99%

“…The former reaction of the pathway was catalyzed by an ␣-ketoglutarate (␣KG)-dependent L-Ile dioxygenase (IDO) (18) and the latter by a NAD ϩ -dependent HIL dehydrogenase (23). In addition, we developed an efficient production system for HIL using Escherichia coli cells heterologously expressing IDO (31).…”

mentioning

confidence: 99%

Characterization of Bacillus thuringiensis l -Isoleucine Dioxygenase for Production of Useful Amino Acids

Hibi

Kawashima

Kodera

et al. 2011

Appl Environ Microbiol

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“…According to the previous researches, the N-terminal amino acid residue of the mature IDO isolated from B. thuringiensis strain 2e2 was Lys, and the first 6 amino acid residues of the initially translated protein (MTFVLS) were cleaved to generate the mature form (Kodera et al 2009;Smirnov et al 2010). Therefore, the truncated IdoΔ6 which lacks the 2-6 amino acid residues was then expressed in C. glutamicum ssp.…”

Section: Effects Of Corn Steep Liquor Supplementation On 4-hil Producmentioning

confidence: 99%

“…IDO catalyzes the C-4 hydroxylation of Ile to form 4-HIL with the concomitant oxidation of α-ketoglutarate (KG) to form succinate. Soon afterward, IDO was cloned and expressed in recombinant Escherichia coli to couple the cell growth with Ile hydroxylation and to convert the supplemented Ile into 4-HIL (Smirnov et al 2010;Kivero et al 2012). Finally, 82 and 156 mM 4-HIL was produced from 100 and 200 mM Ile, respectively, by two recombinant E. coli strains.…”

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confidence: 99%

“…lactofermentum strain, a novel strategy based on corn steep liquor limitation was researched. Meanwhile, it had been reported previously that the Bmature^IDO lost the first 6 amino acid residues at N-terminus (Smirnov et al 2010); therefore, the truncated idoΔ6 was expressed in SN01 and 4-HIL biosynthesis in ido-and idoΔ6-expressing strains was compared. After examining the effect of ido and idoΔ6 expression on 4-HIL production, the protein level and enzyme properties of Ido and IdoΔ6 were analyzed.…”

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4-Hydroxyisoleucine production of recombinant Corynebacterium glutamicum ssp. lactofermentum under optimal corn steep liquor limitation

Shi

Niu

Fang

2015

Appl Microbiol Biotechnol

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4-Hydroxyisoleucine (4-HIL) is a nonproteinogenic amino acid that exhibits insulinotropic biological activity. Here, L-isoleucine dioxygenase gene (ido) derived from Bacillus thuringiensis YBT-1520 was cloned and expressed in an L-isoleucine-producing strain, Corynebacterium glutamicum ssp. lactofermentum SN01, in order to directly convert its endogenous L-isoleucine (Ile) into 4-HIL through single-step fermentation. The effects of corn steep liquor limitation as well as ido and truncated idoΔ6 overexpression on 4-HIL production were researched. 4-HIL production by ido-overexpressing strain was improved to 65.44 ± 2.27 mM after fermented for 144 h under corn steep liquor-subsufficient condition, obviously higher than that under corn steep liquor-rich and insufficient conditions. The conversion ratio of Ile to 4-HIL increased to 0.85 mol/mol. In addition, 4-HIL production by ido-overexpressing strain was higher than that by idoΔ6-overexpressing strain, in accord with the relatively higher affinity of Ido as compared to IdoΔ6. This research generated a novel system for 4-HIL de novo biosynthesis and demonstrated corn steep liquor limitation as a useful strategy for improving 4-HIL production in recombinant C. glutamicum ssp. lactofermentum.

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Biocatalytic Introduction of Chiral Hydroxy Groups using Oxygenases and Hydratases

2016

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Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-hydroxyisoleucine

Cited by 71 publications

References 18 publications

Characterization of Bacillus thuringiensis l -Isoleucine Dioxygenase for Production of Useful Amino Acids

Characterization of Bacillus thuringiensis l -Isoleucine Dioxygenase for Production of Useful Amino Acids

4-Hydroxyisoleucine production of recombinant Corynebacterium glutamicum ssp. lactofermentum under optimal corn steep liquor limitation

Biocatalytic Introduction of Chiral Hydroxy Groups using Oxygenases and Hydratases

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