1.4.1.9: leucine dehydrogenase
This is an abbreviated version!
For detailed information about leucine dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.9
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1.4.1.9
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sphaericus
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l-valine
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synthesis
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l-isoleucine
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l-2-aminobutyric
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l-tert-leucine
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intermedius
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thermoactinomyces
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l-threonine
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analysis
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space-time
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3.5.1.5
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trimethylpyruvate
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alpha-ketoisocaproate
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lysinibacillus
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drug development
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biotechnology
- 1.4.1.9
- sphaericus
- l-valine
- synthesis
- l-isoleucine
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l-2-aminobutyric
- l-tert-leucine
- intermedius
-
thermoactinomyces
- l-threonine
- analysis
-
space-time
-
3.5.1.5
- trimethylpyruvate
- alpha-ketoisocaproate
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lysinibacillus
- drug development
- biotechnology
Reaction
Synonyms
BCD, dehydrogenase, leucine, L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, LeuDH
ECTree
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Application
Application on EC 1.4.1.9 - leucine dehydrogenase
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analysis
biotechnology
an efficient stereospecific enzymatic synthesis of L-valine, L-leucine, L-norvaline, L-norleucine and L-isoleucine from the corresponding alpha-keto acids by coupling the reactions catalysed by leucine dehydrogenase and glucose dehydrogenase/galactose mutarotase. Giving high yields of L-amino acids, the procedure is economical and easy to perform and to monitor at a synthetically useful scale (1-10 g)
drug development
synthesis
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postcolumn co-immobilized leucine dehydrogenase-NADH oxidase reactor for the determination of branched-chain amino acids by high-performance liquid chromatography with chemiluminescence detection
analysis
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assay of serum and urine for urea with use of urease and leucine dehydrogenase
analysis
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flow-injection determination of branched-chain L-amino acids with immobilized leucine dehydrogenase
analysis
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cheap and rapid determination of branched-chain amino and oxo acids
analysis
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cheap and rapid determination of branched-chain amino and oxo acids
analysis
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high-performance liquid chromatographic determination of branched-chain alpha-keto acids in serum using immobilized leucine dehydrogenase as post-column reactor
construction of bifunctional formate dehydrogenase and leucine dehydrogenase enzymatic complex for efficient cofactor regeneration and L-tert leucine biotransformation. L-tert leucine is a widely used chiral building block in many asymmetric reactions for the synthesis of anti-tumor and anti-HIV drugs
drug development
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construction of bifunctional formate dehydrogenase and leucine dehydrogenase enzymatic complex for efficient cofactor regeneration and L-tert leucine biotransformation. L-tert leucine is a widely used chiral building block in many asymmetric reactions for the synthesis of anti-tumor and anti-HIV drugs
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synthesis of L-selenomethionine from 2-oxo-4-methylselenobutanoate
synthesis
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conversion of ammonia or urea into essential amino acids, L-Leu, L-Val, and L-Ile, using artificial cells containing an immobilized multienzyme system that consists of EC 1.1.1.1, EC 1.4.1.9, EC 3.5.1.5 and dextran-NAD+
synthesis
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production of L-Leu, L-Val and L-Ile by artificial cells containing a glucose dehydrogenase and leucine dehydrogenase
synthesis
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preparation of (S)-1-cyclopropyl-2-methoxyethanamine, a key chiral intermediate for the synthesis of a corticotropin releasing factor-1 (CRF-1) receptor antagonist, by a chemoenzymatic route using leucine dehydrogenase. Synthesis of (S)-1-cyclopropyl-2-methoxyethanamine starting from methylcyclopropyl ketone. Permanganate oxidation of the ketone gives cyclopropylglyoxylic acid, which is converted to (S)-cyclopropylglycine by reductive amination using leucine dehydrogenase from Thermoactinomyces intermedius, recombinantly expressed in Escherichia coli, with NADH cofactor recycling by formate dehydrogenase from Pichia pastoris
synthesis
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coexpression with Bacillus megaterium glucose dehydrogenase in Escherichia coli for the production of L-tert-leucine. A decagram preparation of L-tert-leucine is performed at a substrate concentration of 0.6 M in 1 l scale with 99% conversion after 5.5 h, resulting in 80.1% yield and > 99% enantiomeric excess
synthesis
coexpression with NAD+-dependent FDH from Candida boidinii in Escherichia coli for synthesis of L-tert-leucine. In a continuous feeding process, at an overall substrate concentration up to 1.5 M, both conversion and enantiomeric excess of >99% and space-time yield of 786 g/l/d are achieved
synthesis
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formation of a bifunctional enzyme complex consisting of leucine dehydrogenase (LDH) and formate dehydrogenase from Candida boidinii via a miniscaffoldin for production of L-tert-leucine. Ninety-one grams of L-tert-leucine per liter with an enantiomeric purity of 99% e.e. can be obtained
synthesis
high-throughput screening method for L-tert-leucine synthesis and directed evolution strategy to engineer LeuDH for improved efficiency of L-tert-leucine synthesis
synthesis
production of L-2-aminobutanoate from L-threonine via overexpression of L-threonine deaminase from Escherichia coli, L-leucine dehydrogenase from Bacillus cereus, and formate dehydrogenase from Pseudomonas sp. in Escherichia coli with formate as a cosubstrate for NADH regeneration. 30 mol L-threonine are converted to 29.2 mol L-2-aminobutanoate with 97.3 % theoretical yield and with a productivity of 6.37 g/l/h at 50 l
synthesis
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enzyme cascade from threonine to synthesis of L-2-aminobutanoate. In this cascade, the threonine deaminase is used for threonine to 2-oxobutanoate, then LeuDH mutant and formate dehydrogenase are used for synthesis of L-2-aminobutanoate. Under optimized conditions, 1 M threonine is catalyzed by whole cells of Escherichia coli harboring the enzymes in 12 h in sodium phosphate buffer to the optically pure L-2-aminobutanoate with a yield of 99% and ee above 99%
synthesis
enzyme coupled with recombinant formate dehydrogenase is used to catalyze trimethylpyruvic acid through reductive amination to generate enantiopure L-tert-leucine. Using a fed-batch feeding strategy, up to 0.8 M of trimethylpyruvate is transformed to L-tert-leucine, with an average conversion rate of 81% and L-tert-leucine concentration of 65.6 g/l
synthesis
in Escherichia coli expressing IvlA, mutant K72A, formate dehydrogenase, under optimized conditions 150 g L-threonine is transformed to 121 g L-2-aminobutanoate in 5 l fermenter with 95% molar conversion rate, and a productivity of 5.04 g/l and h
synthesis
production of L-tert-leucine by a fusion enzyme of leucine dehydrogenase and glucose dehydrogenase with a rigid peptide linker (GDH-R3-LeuDH). Compared with the free enzymes, both the environmental tolerance and thermal stability of GDH-R3-LeuDH is improved. The fusion structure accelerates the cofactor regeneration rate and maintains the enzyme activity. The space-time yield of L-tert-leucine synthesis by GDH-R3-LeuDH whole cells is up to 2136 g/l/day in a 200 ml scale system under the optimal conditions (pH 9.0, 30°C, 0.4 mM of NAD+ and 500 mM of substrate including trimethylpyruvic acid and glucose)
synthesis
production of L-tert-leucine. A coupled reaction comprising LeuDH with glucose dehydrogenase of Bacillus amyloliquefaciens results in substrate inhibition at high trimethylpyruvate concentrations (0.5 M), which is overcome by batch-feeding of the substrate. The total turnover number and specific space-time conversion of 0.57 M substrate increases to 11400 and 22.8 mmol per h and l and g, respectively
synthesis
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production of L-valine in Escherichia coli on the base of the aminotransferase B-deficient strain V1 by introducing one chromosomal copy of the Bcd gene or the IlvE gene. The Bcd-possessing strain exhibits 2.2fold higher L-valine accumulation (up to 9.1 g/l) and 2.0fold higher yield (up to 35.3%) under microaerobic conditions than the IlvE-possessing strain
synthesis
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in Escherichia coli expressing IvlA, mutant K72A, formate dehydrogenase, under optimized conditions 150 g L-threonine is transformed to 121 g L-2-aminobutanoate in 5 l fermenter with 95% molar conversion rate, and a productivity of 5.04 g/l and h
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synthesis
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enzyme coupled with recombinant formate dehydrogenase is used to catalyze trimethylpyruvic acid through reductive amination to generate enantiopure L-tert-leucine. Using a fed-batch feeding strategy, up to 0.8 M of trimethylpyruvate is transformed to L-tert-leucine, with an average conversion rate of 81% and L-tert-leucine concentration of 65.6 g/l
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synthesis
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production of L-2-aminobutanoate from L-threonine via overexpression of L-threonine deaminase from Escherichia coli, L-leucine dehydrogenase from Bacillus cereus, and formate dehydrogenase from Pseudomonas sp. in Escherichia coli with formate as a cosubstrate for NADH regeneration. 30 mol L-threonine are converted to 29.2 mol L-2-aminobutanoate with 97.3 % theoretical yield and with a productivity of 6.37 g/l/h at 50 l
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synthesis
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coexpression with NAD+-dependent FDH from Candida boidinii in Escherichia coli for synthesis of L-tert-leucine. In a continuous feeding process, at an overall substrate concentration up to 1.5 M, both conversion and enantiomeric excess of >99% and space-time yield of 786 g/l/d are achieved
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