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Search term: synthesis

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EC Number Recommended Name Application Commentary
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis production of (S)-4-(3,4-methylenedioxyphenyl)-2-propanol, which is converted to LY300164, an orally active benzodiazepine
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis alcohol dehydrogenases represent an important group of biocatalysts due to their ability to stereospecifically reduce prochiral carbonyl compounds
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis overexpression of the adhB gene results in a significant increase in the ethanol level
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis protocol for the synthesis of [4R-(2)H]NADH with high yield by enzymatic oxidation of 2-propanol-d(8)
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol 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
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis the alcohol dehydrogenase from Pyrococcus furiosus is a very robust enzyme in some organic solvents. From a synthetic point of view, this property is particularly important and useful for the reduction of ketones with a low solubility in aqueous buffers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Acetobacter aceti catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Aminobacter aminovorans slightly catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Gluconobacter diazotrophicus slightly catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Komagataeibacter medellinensis catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Komagataeibacter xylinus catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. The enzyme from Acetobacter senegalensis catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase synthesis horse liver alcohol dehydrogenase (HLADH) together with the NADH oxidase from Streptococcus mutans (SmNOX) are applied for the oxidative lactamization of various amino alcohols, direct synthesis of lactams (5-, 6-, and 7-membered) starting from amino-alcohols in a bienzymatic cascade. A direct approach for biocatalytic oxidative lactamization reaction. In situ regeneration of NAD+ with SmNOX in the HLADH-catalyzed oxidative lactamization of 4-amino-1-butanol to gamma-butyrolactam. The bienzymatic reaction cascade exhibits an optimum between pH 8 and pH 10, which can be attributed to the rather narrow pH range of SmNOX compared to that of HLADH. The fast reoxidation of NADH eliminated inhibitory effects of NADH on the HLADH-catalyzed oxidation
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol dehydrogenase (NADP+) synthesis -
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol dehydrogenase (NADP+) synthesis reduction of industrially important compounds cinnamyl aldehyde and anisaldehyde, industrial bioconversion of useful alcohols and aldehydes
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol dehydrogenase (NADP+) synthesis useful for asymmetric production of L-carnitine
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol dehydrogenase (NADP+) synthesis industrial ethanol production
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol 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
Show all pathways known for 1.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.2alcohol dehydrogenase (NADP+) synthesis engineering ADHs for regenerating NADPH by oxidation of diols
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3homoserine 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
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3homoserine dehydrogenase synthesis enzyme HSD is utilized in the large scale production of L-lysine
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(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
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(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
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(S)-specific secondary alcohol dehydrogenase synthesis the enzyme is useful in production of chiral compounds for organic synthesis
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(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%
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(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
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(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
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(S)-specific secondary alcohol dehydrogenase synthesis the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, the activity is 6.2 U/mg. Using two coexisting recombinant Escherichia coli strains, in which a strain expressing glucose dehydrogenase is used as an NADPH regenerator. An optical purity of 99% (e.e.) and a maximum yield of 1240 mM (S)-4-chloro-3-hydroxybutanoate are obtained, and highest turnover number of 53900 can be achieved without adding extra NADP+/NADPH
Show all pathways known for 1.1.1.B3Display the reaction diagram Show all sequences 1.1.1.B3(S)-specific secondary alcohol dehydrogenase synthesis using recombinant Scr2 in an aqueous-organic solvent system with a substrate fed-batch strategy and a final substrate concentration of 1 M, a yield of 95.3% and e.e. of 99% is obtained after 6-h reaction
Show all pathways known for 1.1.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.4(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
Show all pathways known for 1.1.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.4(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
Show all pathways known for 1.1.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.4(R,R)-butanediol dehydrogenase synthesis Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO) and can be utilized for large scale production
Show all pathways known for 1.1.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.4(R,R)-butanediol dehydrogenase synthesis two coexpressed enantiocomplementary carbonyl reductases, BDHA (2, 3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) are used for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity and coupled with cofactor regeneration by GDH. Enantiomerically pure (R)-1-phenyl-1,2-ethanediol ((R)-PED) can be used as a building block for the preparation of (R)-norfluoxetine, (R)-fluoxetine, and beta-lactam antibiotics
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4(R)-specific secondary alcohol dehydrogenase (NADH) synthesis the enzym is useful in production of chiral compounds for organic synthesis
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4(R)-specific secondary alcohol dehydrogenase (NADH) 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
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4(R)-specific secondary alcohol dehydrogenase (NADH) 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%
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4(R)-specific secondary alcohol dehydrogenase (NADH) synthesis using recombinant Escherichia coli cells expressing Sdr, a yield of 82.5% for (R)-[3,5-bis(trifluoromethyl)phenyl]ethanol can be achieved within 12 h at a substrate concentration of up to 1000 M
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4(R)-specific secondary alcohol dehydrogenase (NADH) synthesis the enzyme is coupled with formate dehydrogenase and co-immobilized on SiO2 particles, the system is used for continuous catalytic conversion of beta-hydroxyacetophenone to optically pure (r)-phenylethanediol with in situ NADH regeneration and recycling. Reusable system, method overview
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4(R)-specific secondary alcohol dehydrogenase (NADH) synthesis the enzyme might be useful in application as a replacement of chemical synthesis of aromatic chiral beta-amino alcohols
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis biotransformation of glycerol to dihydroxyacetone by recombinant Gluconobacter oxydans DSM 2343. Overproduction of the glycerol dehydrogenase to improve production of dihydroxyacetone
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol 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
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis efficiency of a cofactor regeneration enzyme co-expressed with a glycerol dehydrogenase for the production of 1,3-dihydroxyacetone. In vitro biotransformation of glycerol is achieved with the cell-free extracts containing recombinant glycerol dehydrogenase from Escherichia coli, lactate dehydrogenase form Bacillus subtilis, or NADH oxidase LpNox1 from Lactobacillus pentosus, giving1,3-dihydroxyacetone (DHA), no expensive consumption of NAD+ for the production of DHA, overview. DHA is a valuable chemical with a wide range of applications in the cosmetics
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis engineering and immobilizing of glycerol dehydrogenase to accept alkyl/aryl glyceryl monoethers and catalyze their enantioselective oxidation to yield the corresponding 3-alkoxy/aryloxy-1-hydroxyacetones. The enzyme is highly enantioselective towards S-isomers (ee > 99%). Application of mutant L252A in a one-pot chemoenzymatic process to convert glycidol and ethanol into 3-ethoxy-1-hydroxyacetone and (R)-3-ethoxypropan-1,2-diol, without affecting the oxidation activity
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis engineering of a hypertransformable variant of Clostridium pasteurianum for bioconversion of glycerol into hydrogen via increasing product yield by overexpression of enzyme catalyzing H2 production, and increasing substrate uptake by overexpression of enzymes involved in glycerol utilization. Overexpression of the HydA gene encoding hydrogenase, and overexpression of DhaD1 and DhaK genes encoding glycerol dehydrogenase and dihydroxyacetone kinase result in two recombinant strains (HydA++/HhaD1K++) capable of producing 97% H2 (v/v), with yields of 1.1 mol H2/mol glycerol in HydA overexpressed strain, and 0.93 mol H2/mol glycerol in DhaD1K overexpressing strain
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis immobilization of Escherichia coli cells harboring the recombinant glycerol dehydrogenase gene on mannose-functionalized magnetic nanoparticles for conversion of glycerol to 1,3-dihydroxyacetone. Immobilization uses specific binding between mannose on the nanoparticles and the FimH lectin on the Escherichia coli cell surface via hydrogen bonds and hydrophobic interactions. Compared with the free cells, the thermostability of the immobilized cells is improved 2.56fold at 37°C. More than 50% of the initial activity of the immobilized cells remains after 10 cycles
Show all pathways known for 1.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.6glycerol dehydrogenase synthesis regeneration of NAD+ in enzyme-catalyzed reactions using aggreagets of glycerol dehydrogenase and NADH oxidase. After optimization, the activities of combi-aggregates and separate aggregates mixtures are 950 and 580 U/g, respectively. After ten cycles of reuse, the catalytic efficiency may still retain 63.3% of its initial activity. The conversion of glycerol to 1,3-dihydroxyacetone is 4.6%, which is 2.5 times of the free enzyme system
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.8glycerol-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
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.8glycerol-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
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.8glycerol-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
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.8glycerol-3-phosphate dehydrogenase (NAD+) synthesis Camelina sativa coexpressing Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and yeast cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-coexpressing lines is almost twofold higher as compared to wild type and the lines expressing DGAT1 and GPD1 alone
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.8glycerol-3-phosphate dehydrogenase (NAD+) synthesis upon heterologous expression of diacylglycerol acyltransferase DGAT1, glycerol-3-phosphate dehydrogenase GPD1 and DGAT1 + GPD1 in Camelina sativa, increase in triacylglycerol production is limited by utilization of fixed carbon from the source tissues supported by the increase in glycolysis pathway metabolites and decreased transcripts levels of transcription factors controlling fatty acids synthesis, and triacylglycerol accumulation is limited by the activity of lipases/hydrolases that hydrolyze triacylglycerol pool supported by the increase in free fatty acids and monoacylglycerols
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-xylulose reductase synthesis optimization of xylitol production, using fed-batch process and controlled pH 6.0 gives maximum enzyme activity
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-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
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-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
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-xylulose reductase synthesis the enzyme is useful for xylitol bioproduction, profiles, overview
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-xylulose reductase synthesis Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-xylulose reductase synthesis enzyme IoXyl2p from Issatchenkia orientalis is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
Show all pathways known for 1.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.9D-xylulose reductase synthesis enzyme TdXyl2p from Torulaspora delbrueckii is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.10L-xylulose reductase synthesis the microalga Chlorella sorokiniana and provide a target for genetic engineering to improve D-xylose utilization for microalgal lipid production
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.10L-xylulose reductase synthesis potential approach for industrial-scale production of xylitol from hemicellulosic hydrolysate involving the enzyme
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.12L-arabinitol 4-dehydrogenase synthesis immobilization of HjLAD onto silicon oxide nanoparticles has the potential for use in the industrial production of rare sugars, e.g. L-xylulose, due to the thermostability and reusability of the immobilized enzyme
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.12L-arabinitol 4-dehydrogenase synthesis rare L-sugar L-xylulose is produced by the enzymatic oxidation of arabinitol to give a yield of approximately 86%
Show all pathways known for 1.1.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.14L-iditol 2-dehydrogenase synthesis L-sorbose is an important intermediate in the industrial vitamin C production process
Show all pathways known for 1.1.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.14L-iditol 2-dehydrogenase synthesis two co-expressed enantiocomplementary carbonyl reductases, BDHA (2,3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) are used for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity and coupled with cofactor regeneration by GDH. Enantiomerically pure (R)-1-phenyl-1,2-ethanediol ((R)-PED) can be used as a building block for the preparation of (R)-norfluoxetine, (R)-fluoxetine, and beta-lactam antibiotics
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.16galactitol 2-dehydrogenase synthesis the enzyme can be used to produce optically pure building blocks and for the bioconversion of bioactive compounds
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.16galactitol 2-dehydrogenase synthesis a yeast strain capable of consuming lactose intracellularly is engineered to produce tagatose from lactose. GAL1 coding for galactose kinase is deleted to eliminate galactose utilization. Heterologous xylose reductase (XR) and galactitol dehydrogenase (GDH) are introduced into the Gal1 deletion strain. The expression levels of XR and GDH are adjusted to maximize tagatose production. The resulting engineered yeast produces 37.69 g/l of tagatose from lactose with a tagatose and galactose ratio of 9:1 in the reaction broth
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