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Search term: synthesis

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EC Number
Application
Commentary
alcohol dehydrogenase
synthesis
production of (S)-1-Phenyl-2-propanol, which is used as an intermediate for the synthesis of amphetamines and as a precursor for anti-hypertensive agents and spasmolytics or anti-epileptics
alcohol dehydrogenase
synthesis
production of (S)-4-(3,4-methylenedioxyphenyl)-2-propanol, which is converted to LY300164, an orally active benzodiazepine
alcohol dehydrogenase
synthesis
production of (3R,5S)-6-benzyloxy-3,5-dihydroxy-hexanoic acid ethyl ester, which is a key chiral intermediate for anticholesterol drugs that act by inhibition of hydroxy methyl glutaryl coenzyme A reductase
alcohol dehydrogenase
synthesis
production of (4S,6S)-5,6-dihydro-4-hydroxy-6-methyl-4H-thieno[2,3b]thiopyran-7,7dioxide, which is an intermediate in the synthesis of the carbonic anhydrase inhibitor trusopt. Trusopt is a novel, topically active treatment for glaucoma
alcohol dehydrogenase
synthesis
enzyme catalyzes the following reactions with Prelog specificity: the reduction of acetophenone, 2,2,2-trifluoroacetophenone, alpha-tetralone, and alpha-methyl and alpha-ethyl benzoylformates to (S)-1-phenylethanol (>99% enantiomeric excess), (R)-alpha-(trifluoromethyl)benzyl alcohol (93% enantiomeric excess), (S)-alpha-tetralol (>99% enantiomeric excess), methyl (R)-mandelate (92% enantiomeric excess), and ethyl (R)-mandelate (95% enantiomeric excess), respectively, by way of an efficient in situ NADH-recycling system involving 2-propanol and a second thermophilic ADH
alcohol dehydrogenase
synthesis
yeast alcohol dehydrogenase with its cofactor NAD+ can be stably encapsulated in liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The liposomes are 100 nm in mean diameter, the liposomal ADH and NAD+ concentrations are 2.3 mg/ml and 3.9 mM, respectively. Free ADH is increasingly deactivated during its incubation at 45°C for 2 h with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric ADH into its subunits. Both liposomal enzyme systems, in presence and absence of NAD+, show stabilities at both 45 and 50°C much higher than those of the free enzyme systems, implying that the liposome membranes stabilize the enzyme tertiary and quaternary structures. The enzyme activity of the liposomes in presence of NAD+ show a stability higher than that in absence of NAD+ with a more remarkable effect of NAD+ at 50°C than at 45°C
alcohol dehydrogenase
synthesis
the photochemical and enzymatic synthesis of methanol from formaldehyde with alcohol dehydrogenase and NAD+ photoreduction by the visible-light photosensitization of zinc tetraphenylporphyrin tetrasulfonate in the presence of methylviologen, diaphorase, and triethanolamine is developed
alcohol dehydrogenase
synthesis
synthesis of the cinnamyl alcohol by means of enzymatic reduction of cinnamaldehyde using alcohol both as an isolated enzyme, and in recombinant Escherichia coli whole cells in an efficient and sustainable one-phase system. The reduction of cinnamaldehyde (0.5 g/l, 3.8 mmol/l) by the isolated enzyme occurrs in 3 h at 50°C with 97% conversion, and yields high purity cinnamyl alcohol (98%) with a yield of 88% and a productivity of 50 g/g enzyme. The reduction of 12.5 g/l (94 mmol/l) cinnamaldehyde by whole cells in 6 h, at 37°C and no requirement of external cofactor occurrs with 97% conversion, 82% yield of 98% pure alcohol and a productivity of 34 mg/g wet cell weight
alcohol dehydrogenase
synthesis
immobilization of enzyme on metal-derivatized epoxy Sepabeads. The highest immobilization efficiency (100%) and retention activity (60%) are achieved after 48 h of incubation of the enzyme with Niepoxy Sepabeads support in 100 mM Tris-HCl buffer, pH 8, containing 3 M KCl at 5°C. A significant increase in the stability of the immobilized enzyme is achieved by blocking the unreacted epoxy groups with ethylamine. The immobilization process increases the enzyme stability, thermal activity, and organic solvents. One step purification-immobilization can be carried out on metal chelate-epoxy Sepabeads
alcohol dehydrogenase
synthesis
synthetic pathway for n-butanol production from acetyl coenzyme at 70°C, using beta-ketothiolase Thl, 3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA dehydratase Crt from Caldanaerobacter subterraneus subsp. tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta thermophila and bifunctional aldehyde dehydrogenase AdhE and and butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, is used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol is observed in vitro, but with a 60% decrease in the predicted pathway flux
alcohol dehydrogenase
synthesis
semi-preparative biocatalysis at 60°C using the stabilized mutant C257L, employing butyraldehyde for in situ cofactor regeneration with only catalytic amounts of NAD+, yields up to 23% conversion of omega-hydroxy lauric acid methyl ester to omega-oxo lauric acid methyl ester after 30 min
alcohol dehydrogenase
synthesis
recombinant enzyme activity can be improved by coexpression of archaeal chaperones (i.e., gamma-prefoldin and thermosome). Ricinoleic acid biotransformation activity of recombinant Escherichia coli expressing Micrococcus luteus alcohol dehydrogenase and the Pseudomonas putida KT2440 Baeyer-Villiger monooxygenase improves significantly with coexpression of gamma-prefoldin or recombinant themosome originating from the deep-sea hyperthermophile archaea Methanocaldococcus jannaschii. The degree of enhanced activity is dependent on the expression levels of the chaperones
alcohol dehydrogenase
synthesis
simplified production scheme for isobutanol based on a cell-free immobilized enzyme system. Immobilized enzymes keto-acid decarboxylase (KdcA) and alcohol dehydrogenase (ADH) plus formate dehydrogenase (FDH) for NADH recycle in solution produce isobutanol titers 8 to 20 times higher than the highest reported titers with Saccharomyces cerevisiae on a mol/mol basis. Conversion rates and low protein leaching are achieved by covalent immobilization on methacrylate resin. The enzyme system without in situ removal of isobutanol achieves a 55% conversion of ketoisovaleric acid to isobutanol at a concentration of 0.135 mol isobutanol produced for each mol ketoisovaleric acid consumed
alcohol dehydrogenase
synthesis
in order to increase production of isobutanol, 2-oxoacid decarboxylase (KDC) and alcohol dehydrogenase (ADH) are expressed in Saccharomyces cerevisiae to enhance the endogenous activity of the Ehrlich pathway. Overexpression Ilv2, which catalyzes the first step in the valine synthetic pathway, and deletion of the PDC1 gene encoding a major pyruvate decarboxylase alters the abundant ethanol flux via pyruvate. Along with modification of culture conditions, the isobutanol titer is elevated 13fold, from 11 mg/l to 143 mg/l, and the yield is 6.6 mg/g glucose
alcohol dehydrogenase
synthesis
alpha-ketoisovalerate decarboxylase Kivd from Lactococcus lactis combined with alcohol dehydrogenase Adh3 from Zymomonas mobilis are the optimum candidates for 3-methyl-1-butanol production in Corynebacterium glutamicum. The recombinant strain produces 0.182 g/l of 3-methyl-1-butanol and 0.144 g/l of isobutanol after 12 h of incubation. Further inactivation of the E1 subunit of pyruvate dehydrogenase complex gene (aceE) and lactic dehydrogenase gene (ldh) improves the 3-methyl-1-butanol titer to 0.497 g/l after 12 h of incubation
alcohol dehydrogenase
synthesis
construction of a synthetic pathway for bioalcohol production at 70°C by insertion of the gene for alcohol dehydrogenase AdhA into the archaeon Pyrococcus furiosus. The engineered strain converts glucose to ethanol via acetate and acetaldehyde, catalyzed by the host-encoded aldehyde ferredoxin oxidoreductase AOR and heterologously expressed AdhA, in an energy-conserving, redox-balanced pathway. The AOR/AdhA pathway also converts exogenously added aliphatic and aromatic carboxylic acids to the corresponding alcohol using glucose, pyruvate, and/or hydrogen as the source of reductant. By heterologous coexpression of a membrane-bound carbon monoxide dehydrogenase, CO is used as a reductant for converting carboxylic acids to alcohols
alcohol dehydrogenase
synthesis
protocol for the synthesis of [4R-(2)H]NADH with high yield by enzymatic oxidation of 2-propanol-d(8)
alcohol dehydrogenase
synthesis
under optimized conditions, the enzyme produces 600 mg all-trans-retinol per l after 3 h, with a conversion yield of 27.3% (w/w) and a productivity of 200 mg per l and h
alcohol dehydrogenase
synthesis
engineering of a strain of Corynebacterium glutamicum, based on inactivation of the pyruvate dehydrogenase complex, pyruvate:quinone oxidoreductase, transaminase B, and additional overexpression of the IlvBNCD genes, encoding acetohydroxyacid synthase, acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase, for the production of isobutanol from glucose under oxygen deprivation conditions by inactivation of L-lactate and malate dehydrogenases, implementation of ketoacid decarboxylase from Lactococcus lactis, alcohol dehydrogenase 2 (ADH2) from Saccharomyces cerevisiae, and expression of the pntAB transhydrogenase genes from Escherichia coli. The resulting strain produces isobutanol with a substrate-specific yield (YP/S) of 0.60 mol per mol of glucose. Chromosomally encoded alcohol dehydrogenase AdhA rather than the plasmid-encoded ADH2 from Saccharomyces cerevisiae is involved in isobutanol formation, and overexpression of the corresponding AdhA gene increases the YP/S to 0.77 mol of isobutanol per mol of glucose. Inactivation of the malic enzyme significantly reduces the YP/S, indicating that the metabolic cycle consisting of pyruvate and/or phosphoenolpyruvate carboxylase, malate dehydrogenase, and malic enzyme is responsible for the conversion of NADH + H+ to NADPH + H+. In fed-batch fermentations with an aerobic growth phase and an oxygen-depleted production phase, the most promising strain produces about 175 mM isobutanol, with a volumetric productivity of 4.4 mM per h, and shows an overall YP/S of about 0.48 mol per mol of glucose in the production phase
alcohol dehydrogenase
synthesis
engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (IlvH), keto-acid reducto-isomerase (IlvC) and dihydroxyacid dehydratase (IlvD) from Klebsiella pneumoniae, and alpha-oxoisovalerate decarboxylase (Kivd) and alcohol dehydrogenase (AdhA) from Lactococcus lactis. The engineered strain produce 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway by inactivating alpha-acetolactate decarboxylase (Adc) further improves the yield of 2-butanol from 160 to 320 mg/l
alcohol dehydrogenase
synthesis
LSADH catalyzed the enantioselective reduction of some ketones with high enantiomeric excesses: phenyl trifluoromethyl ketone to (S)-1-phenyltrifluoroethanol (>99% e.e.), acetophenone to (R)-1-phenylethanol (99% e.e.), and 2-heptanone to (R)-2-heptanol (>99% e.e.) in the presence of 2-propanol without an additional NADH regeneration system. Therefore, it would be a useful biocatalyst
alcohol dehydrogenase
synthesis
alcohol dehydrogenases represent an important group of biocatalysts due to their ability to stereospecifically reduce prochiral carbonyl compounds; expression of enzyme in auxotrophic Arxula adeninivorans, Hansenula polymorpha, and Saccharomyces cerevisiae strains using yeast ribosomal DNA integrative expression cassettes. Recombinant ADH accumulates intracellularly in all strains tested. The best yields of active enzyme are obtained from A. adeninivorans, with Saccharomyces cerevisiae producing intermediate amounts. Although Hansenula polymorpha is the least efficient producer overall, the product obtained is most similar to the enzyme synthesized by Rhodococcus ruber 219 with respect to its thermostability
alcohol dehydrogenase
synthesis
enzyme can be used in preparative scale enantioselective oxidation of sec-alcohol in asymmetric reduction of ketones, using acetone and 2-propanol, respectively, as cosubstrates for cofactor-regeneration via a coupled-substrate approach
alcohol dehydrogenase
synthesis
deletion of the hypoxanthine phosphoribosyltransferase gene in ethanol tolerant strain adhE*(EA), carrrying mutation P704L/H734R in the alcohol dehydrogenase gene, and deletion of lactate dehydrogenase (ldh) to redirect carbon flux towards ethanol reults in a strain producing 30% more ethanol than wild type on minimal medium. The engineered strain retains tolerance to 5% v/v ethanol, resulting in an ethanol tolerant platform strain
alcohol dehydrogenase
synthesis
overexpression of the adhB gene results in a significant increase in the ethanol level
alcohol dehydrogenase
synthesis
enzyme catalyses the reduction of alpha-methyl and alpha-ethyl benzoylformate, and methyl o-chlorobenzoylformate with 100% conversion to methyl (S)-mandelate [17% enantiomeric excess (ee)], ethyl (R)-mandelate (50% ee), and methyl (R)-o-chloromandelate (72% ee), respectively, with an efficient in situ NADH-recycling system which involves glucose and a thermophilic glucose dehydrogenase
alcohol dehydrogenase
synthesis
construction of an enzyme-immobilized bioanode that can operate at high temperatures. The catalytic current for ethanol oxidation at Ru complex-modified electrodes increases at 80°C up to 12fold compared with room temperature
alcohol dehydrogenase
synthesis
enhancement of ethanol production capacity of Clostridium thermocellum by transferring pyruvate decarboxylase and alcohol dehydrogenase genes of the homoethanol pathway from Zymomonas mobilis. Both transferring pyruvate decarboxylase and alcohol dehydrogenase are functional in Clostridium thermocellum, but the presence of and alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene. The recombinant strain shows two-fold increase in pyruvate carboxylase activity and ethanol production when compared with the wild type strain; expression of pyruvate decarboxylase and alcohol dehydrogenase in Clostridium thermocellum DSM 1313. Though both enzymes are functional in Clostridium thermocellum, the presence of alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene
alcohol dehydrogenase (NADP+)
synthesis
-
alcohol dehydrogenase (NADP+)
synthesis
potential use for industrial production of ethanol by fermentation, thermophilic fermentations offer the potential to separate ethanol from continous cultures at process temperature and reduced pressure during growth
alcohol dehydrogenase (NADP+)
synthesis
industrial ethanol production
alcohol dehydrogenase (NADP+)
synthesis
conversion of prochiral ketones to chiral alcohols by Escherichia coli coexpressing enzyme with NAD+-dependent formate dehydrogenase and pyridine nucleotide transhydrogenase genes pnta and pntb, conversion of 66% acetophenone to (R)-phenylethanol over 12 h
alcohol dehydrogenase (NADP+)
synthesis
the NADP(H)-dependent enzyme is useful in the selective chemoenzymatic synthesis of the tert-butyl (S)-6-chloro-5-hydroxy-3-ketohexanoate, a highly regio- and enantioselective reduction of a beta,delta-diketohexanoate ester, scale up of the continous fed-batch method, overview
alcohol dehydrogenase (NADP+)
synthesis
synthetic pathway for bioalcohol production at 70°C by insertion of the gene for bacterial alcohol dehydrogenase AdhA into the archaeon Pyrococcus furiosus. The engineered strain converts glucose to ethanol via acetate and acetaldehyde, catalyzed by the host-encoded aldehyde ferredoxin oxidoreductase AOR and heterologously expressed AdhA, in an energy-conserving, redox-balanced pathway. The AOR/AdhA pathway also converts exogenously added aliphatic and aromatic carboxylic acids to the corresponding alcohol using glucose, pyruvate, and/or hydrogen as the source of reductant. By heterologous coexpression of a membrane-bound carbon monoxide dehydrogenase, CO is used as a reductant for converting carboxylic acids to alcoholsThe AOR/AdhA pathway is a potentially game-changing strategy for syngas fermentation, especially in combination with carbon chain elongation pathways
alcohol dehydrogenase (NADP+)
synthesis
overexpression of the endogenous zwf gene, which encodes glucose-6-phosphate dehydrogenase of the pentose phosphate pathway, in Synechocystis sp. PCC 6803 results in increased NADPH production, and promoted biomass production. Ethanol production by alcohol dehydrogenase YqhD is increased in autotrophic conditions by zwf overexpression
alcohol dehydrogenase (NADP+)
synthesis
develpoment of conversion processes for petrochemicals and oil-contaminated environments, cinnamyl aldehyde and cinnamyl alcohol used in flavor and perfume industry, anisaldehyde is used for perfume and toilet soaps, decylalcohol is used in the manufacture of plasticizers, a production system for this enzyme may be useful for industrial application as a biocatalyst in the future; reduction of industrially important compounds cinnamyl aldehyde and anisaldehyde, industrial bioconversion of useful alcohols and aldehydes
alcohol dehydrogenase (NADP+)
synthesis
50 microg of alcohol dehydrogenase AdhA, EC 1.1.1.2, and 50 microg actaldehyde dehydrogenase AldH, EC 1.2.1.10,in buffer solution (pH 8.0) containing NADPH, NADH and acetyl-CoA at 60°C, produce 1.6 mM ethanol from 3 mM acetyl-CoA after 90 min
alcohol dehydrogenase (NADP+)
synthesis
useful for asymmetric production of L-carnitine
alcohol dehydrogenase (NADP+)
synthesis
industrial ethanol production; potential use for industrial production of ethanol by fermentation, thermophilic fermentations offer the potential to separate ethanol from continous cultures at process temperature and reduced pressure during growth
alcohol dehydrogenase (NADP+)
synthesis
expression of BdhA enzyme in Caldicellulosiruptor bescii confers increased resistance of the engineered strain to both furfural and 5-hydroxymethylfurfural. In presence of 15 mM of either furan aldehyde, the ability to eliminate furfural or 5-hydroxymethylfurfural from the culture medium is significantly improved in the engineered strain
homoserine dehydrogenase
synthesis
contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
(S)-specific secondary alcohol dehydrogenase
synthesis
the enzyme is useful in production of chiral compounds for organic synthesis
(S)-specific secondary alcohol dehydrogenase
synthesis
synthesis of (R)-1,3-butanediol from its racemate by stereoselective oxidation of the (S)-isomer using (S)-specific secondary alcohol dehydrogenase in whole recombinant Escherichia coli cells. Yield of the (R)-product reaches 72.6 g/l, with a molar recovery yield of 48.4% and an optical purity of 95% enantiomeric excess
(S)-specific secondary alcohol dehydrogenase
synthesis
production of ethyl (R)-4-chloro-3-hydroxybutanoate using whole recombinant cells of Escherichia coli and 2-propanol as an energy source to regenerate NADH. Yield reaches 36.6 g/l with purity of more than 99% enantiomeric excess and 95.2% conversion
(S)-specific secondary alcohol dehydrogenase
synthesis
the immobilized enzyme is utilized in the asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%
(S)-specific secondary alcohol dehydrogenase
synthesis
synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate in Escherichia coli. Coexpression of carbonyl reductase CRII and a glucose dehydrogenase gives an activity of 15 U/mg protein using ethyl 4-chloro-3-oxobutanoate as a substrate in a water/butyl acetate system. The transformants give a molar yield of 91%, and an optical purity of the (S)-isomer of more than 99% enantiomeric excess
(S)-specific secondary alcohol dehydrogenase
synthesis
the enzyme can be used for stereospecific interconversion of (R)-1-phenylethanol and (S)-1-phenylethanol via the oxoform together with the (R)-specific secondary alcohol dehydrogenase using whole cells as biocatalysts that include the required cofactor regenration system, method, overview. Optically pure secondary alcohols are widely used in pharmaceuticals, flavors, agricultural chemicals and specialty materials
(R,R)-butanediol dehydrogenase
synthesis
increase in production of (R,R)-butanediol from xylose in batch and continuous cultures by increase of temperature from 30 to 39°C, analysis of byproducts
(R,R)-butanediol dehydrogenase
synthesis
the enzyme is useful in production of 2,3-butanediol, an important starting material for the manufacture of bulk chemicals such as methyl ethyl ketone and 1,3-butadiene
(R)-specific secondary alcohol dehydrogenase
synthesis
the enzym is useful in production of chiral compounds for organic synthesis
(R)-specific secondary alcohol dehydrogenase
synthesis
ethyl benzoylformate is asymmetrically reduced by the purified enzyme, using an additional coupled NADH regeneration system, with 95% conversion and in an enantiomeric excess of 99.9%
(R)-specific secondary alcohol dehydrogenase
synthesis
the enzyme can be used for stereospecific interconversion of (R)-1-phenylethanol and (S)-1-phenylethanol via the oxoform together with the (S)-specific secondary alcohol dehydrogenase using whole cells as biocatalysts that include the required cofactor regenration system, method, overview. Optically pure secondary alcohols are widely used in pharmaceuticals, flavors, agricultural chemicals and specialty materials
glycerol dehydrogenase
synthesis
biotransformation of glycerol to dihydroxyacetone by recombinant Gluconobacter oxydans DSM 2343. Overproduction of the glycerol dehydrogenase to improve production of dihydroxyacetone
glycerol dehydrogenase
synthesis
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, heterologous gene GldA is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
glycerol dehydrogenase
synthesis
high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds
glycerol-3-phosphate dehydrogenase (NAD+)
synthesis
fermentative production of L-glycerol 3-phosphate utilizing a Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic pathway (strain with deletions in both genes encoding specific L-G3Pases (GPP1 and GPP2) and multicopy overexpression of L-glycerol 3-phosphate dehydrogenase). Up-scaling the process employs fed-batch fermentation with repeated glucose feeding, plus an aerobic growth phase followed by an anaerobic product accumulation phase. This produces a final product titer of about 325 mg total L-glycerol 3-phosphate per liter of fermentation broth
glycerol-3-phosphate dehydrogenase (NAD+)
synthesis
deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations
glycerol-3-phosphate dehydrogenase (NAD+)
synthesis
successful introduction of a glycerol production pathway into Klebseiella pneumoniae by coexpression of genes encoding glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase (EC 3.1.3.21) organized into the plasmid pUC18K under control of the respective lac promoter. An engineered Klebsiella pneumoniae that can produce glycerol from glucose is achieved. It is still difficult to efficiently produce 1,3-propanediol from glucose. Only 0.58 g/l 1,3-propanediol is produced
D-xylulose reductase
synthesis
use of enzyme in xylose fermentation, metabolic flux partitioning from xylitol to xylulose depends on aeration and enzyme activity, increased aeration results in less xylitol accumulation and more xylulose accumulation, increase in enzyme activity can reduce xylitol formation
D-xylulose reductase
synthesis
use of enzyme in production of xylitol from bagasse hydrolysate, enzyme activity is higher in medium containing acetic acid than in control medium
D-xylulose reductase
synthesis
optimization of xylitol production, using fed-batch process and controlled pH 6.0 gives maximum enzyme activity
D-xylulose reductase
synthesis
Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
D-xylulose reductase
synthesis
the enzyme is useful for xylitol bioproduction, profiles, overview
L-iditol 2-dehydrogenase
synthesis
L-sorbose is an important intermediate in the industrial vitamin C production process
mannitol-1-phosphate 5-dehydrogenase
synthesis
strategy for mannitol production in Lactococcus, most promising is overexpression of enzyme in a lactate-dehydrogenase deficient strain
mannitol-1-phosphate 5-dehydrogenase
synthesis
hydrogen transfer from formate to D-fructose 6-phosphate, mediated by NAD(H) and catalyzed by a coupled enzyme system of purified Candida boidinii formate dehydrogenase and AfM1PDH, is used for the preparative synthesis of D-mannitol 1-phosphate or, by applying an analogous procedure using deuterio formate, the 5-[2H] derivative thereof, overview
L-1-amino-2-propanol dehydrogenase
synthesis
coversion of 1-(3-hydroxyphenyl)-2-(methylamino) ethanone to (S)-phenylephrine with with more than 99% enantiomeric excess, 78% yield and a productivity of 3.9 mmol(S)-phenylepinephrine/l h in 12 h at 30°C and pH 7. The (S)-phenylepinephrine, recovered from reaction mixture by precipitation at pH 11.3, can be converted to (R)-phenylepinephrine by Walden inversion reaction
xylitol dehydrogenase (NAD+)
synthesis
production of L-xylulose from xylitol using a resting cell reaction leads to 35% L-xylulose within 24 h, starting from 5% xylitol as initial concentration
aldehyde reductase
synthesis
homochiral 3-hydroxy-4-substituted beta-lactams serve as precursors to the corresponding alpah-hydroxy-beta-amino acids, the enzyme might be useful insynthesis of these key components of many biologically and therapeutically important compounds
L-lactate dehydrogenase
synthesis
the enzyme has a commercial significance, as it can be used to produce chiral building blocks for the synthesis of key pharmaceuticals and agrochemicals, optimization of enzyme reaction by engineering to eliminate the substrate inhibition
L-lactate dehydrogenase
synthesis
development of yeast-based bioprocesses to produce lactate from lignocellulosic raw material
L-lactate dehydrogenase
synthesis
construction of a markerless strain lacking phosphotransacetylase Pta, acetate kinase Ack and lactate dehydrogenase Ldh genes. The gene deletion strain ferments 50 g/liter of cellobiose, with a yield of 0.44 g ethanol per g glucose equivalent substrate and a maximum volumetric productivity of 1.13 g ethanol per liter and h. A system for genetic marker removal allows for enactment of further modifications and creation of strains for industrial applications
L-lactate dehydrogenase
synthesis
metabolic engineering of Geobacillus thermoglucosidasius to divert the fermentative carbon flux from a mixed acid pathway, to one in which ethanol becomes the major product, involving elimination of the lactate dehydrogenase and pyruvate formate lyase pathways by disruption of the ldh and pflB genes, respectively, and upregulation of expression of pyruvate dehydrogenase. Strains with all three modifications form ethanol efficiently and rapidly at temperatures in excess of 60°C in yields in excess of 90% of theoretical. The strains also efficiently ferment cellobiose and a mixed hexose and pentose feed
L-lactate dehydrogenase
synthesis
the enzyme might be useful in the production of phenyllactate
L-lactate dehydrogenase
synthesis
a lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) deletion strain is evolved for 2,000 h, resulting in a stable strain with 40:1 ethanol selectivity and a 4.2-fold increase in ethanol yield over the wild-type strain. In a coculture of organic acid-deficient engineered strains of both Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, fermentation of 92 g/liter Avicel results in 38 g/liter ethanol, with acetic and lactic acids below detection limits, in 146 h. engineering is based on a phosphoribosyl transferase (Hpt) deletion strain, which produces acetate, lactate, and ethanol in a ratio of 1.7:1.5:1.0, similar to the 2.1:1.9:1.0 ratio produced by the wild type. The Hpt/Ldh double mutant strain does not produce significant levels of lactate and has a 1.4:1.0 ratio of acetate to ethanol. Similarly, the Hpt/Pta double mutant strain does not produce acetate and has a 1.9:1.0 ratio of lactate to ethanol. The Hpt/Ldh/Pta triple mutant strain achieves ethanol selectivity of 40:1 relative to organic acids
L-lactate dehydrogenase
synthesis
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, a heterologous gene GldA encoding an NAD+-dependent glycerol dehydrogenase is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant enzyme acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
D-lactate dehydrogenase
synthesis
production of (R)-2-hydroxy-4-phenyl-butyric acid, which is a precursor for different ACE-inhibitors
D-lactate dehydrogenase
synthesis
enzymatic synthesis of (R)-3,4-dihydrixyphenyllactic acid, a pharmacological compound that is used for the treatment of menstrual disorders, menostasis, menorrhalgia, insomnia, blood circulation diseases and Angina pectoris. Regeneration of NADH by formate dehydrogenase system. Use of genetic algorithm as a stochastic optimization method seems to be the best choice for the optimization
3-hydroxybutyrate dehydrogenase
synthesis
the engineered enzyme mutant H144L/W187F is used for production of 4-hydroxyvaleric acid, a monomer of bio-polyester and a precursor of bio-fuels, from levulinic acid
acetoacetyl-CoA reductase
synthesis
PHB-synthesis for thermoplastics
acetoacetyl-CoA reductase
synthesis
establishing of an enzyme-catalyzed synthesis system for production of poly(3-hydroxybutyrate) in vitro on the basis of the poly(3-hydroxybutyrate) biosynthesis pathway of Ralstonia eutropha, recycling CoA for synthesis of acetyl-CoA and deriving NADPH from regeneration by GDH, overview
malate dehydrogenase (decarboxylating)
synthesis
the enzyme is useful for production of L-malic acid with NADH generation including the reverse reaction of malic enzyme and the activity of glucose-6-phosphate dehydrogenase, EC1.1.1.49, from Leuconostoc mesenteroides, overview
phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)
synthesis
thermostability may lead to some practical applications
glucose 1-dehydrogenase [NAD(P)+]
synthesis
usage as NADP+ cofactor regenerator for enzymatic synthesis of chiral compounds such as ethyl-(S)-4-chloro-3-hydroxybutanoate and ethyl 4-chloro-3-oxobutanoate
glucose 1-dehydrogenase [NAD(P)+]
synthesis
enzyme can be used for gluconic acid production in low water systems
glucose 1-dehydrogenase [NAD(P)+]
synthesis
production of recombinant glucose 1-dehydrogenase in Escherichia coli, optimization of culture and induction conditions. Glucose 1-dehydrogenase is used to regenerate NADPH in vivo and in vitro and coupled with a NADPH-dependent bioreduction for efficient synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate from ethyl-4-chloro-3-oxobutanoate
3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)
synthesis
the enzyme is useful foe androsterone production in a coupled system with formate dehydrogenase in enhancing Tris-HCl/co-solvent 1-butyl-3-methylimidazolium L-lactate, at pH 7.6 and 25°C, method optimization, overview; the enzyme is useful in reductive production of steroids. In a coupled-enzyme system comprising HSDH and formate dehydrogenase, a twofold increase in production rate of androsterone is obtained when utilizing 1-butyl-3-methylimidazolium L-lactate with NADH regeneration
3-quinuclidinone reductase (NADPH)
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals
3-quinuclidinone reductase (NADH)
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals
3-quinuclidinone reductase (NADH)
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals. The 3-quinuclidinone reductase and Leifsonia sp. alcohol dehydrogenase genes are efficiently expressed in Escherichia coli cells. A number of constructed Echerichia coli biocatalysts (intact or immobilized) are applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
3-quinuclidinone reductase (NADH)
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals, high yield of (R)-3-quinuclidinol up to 916 g/L * d using a bioreduction approach
3-quinuclidinone reductase (NADH)
synthesis
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals; stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals. The 3-quinuclidinone reductase and Leifsonia sp. alcohol dehydrogenase genes are efficiently expressed in Escherichia coli cells. A number of constructed Echerichia coli biocatalysts (intact or immobilized) are applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(-)-3-quinuclidinolis synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for the immobilized enzyme. The optical purity of the (R)-(-)-3-quinuclidinol produced by the enzymatic reactions is above 99.9%
tagaturonate reductase
synthesis
expression of Lactococcus lactis uxaB and uxaC genes encoding D-tagaturonate reductase and D-galacturonate isomerase, in Saccharomyces cerevisiae to investigate in vivo activity of the first steps of the D-galacturonate pathway. Although D-tagaturonate reductase could, in principle, provide an alternative means for re-oxidizing cytosolic NADH, addition of D-galacturonate does not restore anaerobic growth, possibly due to absence of a functional D-altronate exporter in Saccharomyces cerevisiae
mannitol 2-dehydrogenase
synthesis
the recombinant enzyme expressed in Bacillus megaterium is useful in production of D-mannitol using a resting cell biotransformation approach
gluconate 5-dehydrogenase
synthesis
strain overexpressing enzyme plus Escherichia coli transhydrogenase sthA, enhanced accumulation of 5-ketoD-gluconate, precursor of L-(+)-tartaric acid
(S,S)-butanediol dehydrogenase
synthesis
preparation of chiral acetoinic compounds, enzymic identification for chiral acetoinic compounds or as model enzyme for studying the interrelation between enzymic stereospecificity and structure
(S,S)-butanediol dehydrogenase
synthesis
the key enzymes in the microbial production of 2,3-butanediol
lactaldehyde reductase
synthesis
fermentation of L-rhamnose, L-fucose and D-fucose to a mixture of 1,2-propanediol, acetone, H2, CO2 and ethanol
hydroxypyruvate reductase
synthesis
potential application in the enzymatic synthesis of glyoxylate
aryl-alcohol dehydrogenase
synthesis
biotechnological production of vanillin
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