1.14.11.45: L-isoleucine 4-hydroxylase
This is an abbreviated version!
For detailed information about L-isoleucine 4-hydroxylase, go to the full flat file.
Word Map on EC 1.14.11.45
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1.14.11.45
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4-hydroxyisoleucine
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corynebacterium
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glutamicum
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thuringiensis
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l-ile
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lactofermentum
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insulinotropic
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stereoselectively
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bl21de3
- 1.14.11.45
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4-hydroxyisoleucine
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corynebacterium
- glutamicum
- thuringiensis
- l-ile
- lactofermentum
-
insulinotropic
-
stereoselectively
-
bl21de3
Reaction
Synonyms
IDO, isoleucine 4-hydroxylase, L-isoleucine dioxygenase
ECTree
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Application
Application on EC 1.14.11.45 - L-isoleucine 4-hydroxylase
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synthesis
development of efficient method for the biotransformation of 4-hydroxyisoleucine by resting cells expressing L27I/E80D/G169H/S182D 151.9 mM of 4-hydroxyisoleucine/l (22.4 g/l) can be synthesized in 12 h while the substrates seldom exhibits additional consumption
synthesis
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double mutant I162T/T182N shows improvements in specific activity, protein expression level, and fermentation titer of 3.2-, 2.8-, and 9.4fold, respectively. L-Isoleucine (228 mM) is completely converted to (2S,3R,4S)-4-HIL with a space-time yield of up to 80.8 g/l and d. With a increase of the substrate loading to 1 M, a high conversion of 91% can also be achieved
synthesis
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dynamic regulation of IDO expression by modified Ile biosensors increases the 4-HIL titer from 24.7 mM to 28.9?74.4 mM and may yield more 4-HIL than the static strain overexpressing IDO by the strong PtacM promoter (69.7 mM). Synergistic modulation of 2-oxoglutarate supply and O2 supply improves the 4-HIL production significantly, and the highest titer achieved is 135.3 mM
synthesis
improved synthesis of 4-HIL by ribosomal binding site engineering for gene expression in Corynebacterium glutamicum. To supply the cosubstrate 2-oxoglutarate at different levels, the OdhI gene is expressed using the ribosomal binding site sequences. The O2 supply is further enhanced in by overexpressing the Vgb gene. 4-HIL (up to 119.27 mM) is produced in the best strain. The synchronic supply of cosubstrates 2-oxoglutarate and O2 is critical for the high-yield production of 4-HIL
synthesis
improved synthesis of 4-HIL in an optimized strain of Corynebacterium glutamicum by application of programming adaptive laboratory evolution. The programming evolutionary system contains a Lys biosensor LysG-PlysE and an evolutionary actuator composed of a mutagenesis gene and a fluorescent protein gene. After successive rounds of evolution, mutant strains with significantly increased 4-HIL production and growth performance are obtained. The maximum 4-HIL titer is 152.19 mM, 28.4% higher than the starting strain
synthesis
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in a genome-edited recombinant strain Escherichia coli BL21(DE3) DELTAsucABDeltaaceAK/pET-28a(+)-ido (2DELTA-ido), the bioconversion ratio of L-Ile to 4-HIL is enhanced by about 15% compared to Escherichia coli BL21(DE3)/pET-28a(+)-ido [BL21(DE3)-ido]
synthesis
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recombinant Escherichia coli expressing mutant N126H/T130K or wild-type synthesizes 66.50 mM and 26.09 mM 4-hydroxyisoleucine, respectively, in 24 h