EC Number   |
Recommended Name  |
Application |
|---|
    1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | alcohol dehydrogenase |
synthesis |
production of (S)-4-(3,4-methylenedioxyphenyl)-2-propanol, which is converted to LY300164, an orally active benzodiazepine |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | alcohol dehydrogenase |
synthesis |
alcohol dehydrogenases represent an important group of biocatalysts due to their ability to stereospecifically reduce prochiral carbonyl compounds |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | alcohol dehydrogenase |
synthesis |
overexpression of the adhB gene results in a significant increase in the ethanol level |
| 1.1.1.1 | alcohol dehydrogenase |
synthesis |
protocol for the synthesis of [4R-(2)H]NADH with high yield by enzymatic oxidation of 2-propanol-d(8) |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.10 | L-xylulose reductase |
synthesis |
the microalga Chlorella sorokiniana and provide a target for genetic engineering to improve D-xylose utilization for microalgal lipid production |
| 1.1.1.10 | L-xylulose reductase |
synthesis |
potential approach for industrial-scale production of xylitol from hemicellulosic hydrolysate involving the enzyme |
| 1.1.1.100 | 3-oxoacyl-[acyl-carrier-protein] reductase |
synthesis |
coexpression with fabH mutant F87T and polyhydroxyalkanoate synthase genes enhances the production of short chain length-medium chain length polyhydroxyalkanoate copolymer from both related and unrelated carbon sources. Analysis of polyhydroxyalkanoate accumulation and physical characterization of copolymer |
| 1.1.1.103 | L-threonine 3-dehydrogenase |
synthesis |
over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above |
| 1.1.1.105 | all-trans-retinol dehydrogenase (NAD+) |
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 |
| 1.1.1.108 | carnitine 3-dehydrogenase |
synthesis |
immobilized in nanofiltration membrane bioreactor for the continuous production of L-carnitine |
| 1.1.1.116 | D-arabinose 1-dehydrogenase (NAD+) |
synthesis |
production of L-ascorbic acid and secretion into culture medium by overexpression of enzyme and arabinone-1,4-lactone oxidase in Saccharomyces cerevisiae and Zygosaccharomyces bailii |
| 1.1.1.118 | glucose 1-dehydrogenase (NAD+) |
synthesis |
glucose dehydrogenase and L-carnitine dehydrogenase are coimmobilized in a nanofiltration membrane bioreactor for the continuous production of 1-carnitine from 3-dehydrocarnitine with NADH regeneration |
| 1.1.1.119 | glucose 1-dehydrogenase (NADP+) |
synthesis |
use of enzyme in enzyme-catalyzed synthesis system for poly(3-hydroxybutyrate), enzyme catalyzes regeneration of NADPH, system yields 5.6 mg of poly(3-hydroxybutyrate), in a 5 ml-reaction mixture |
| 1.1.1.119 | glucose 1-dehydrogenase (NADP+) |
synthesis |
Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions |
| 1.1.1.119 | glucose 1-dehydrogenase (NADP+) |
synthesis |
glucose dehydrogenase is generally used to regenerate the expensive cofactor NADPH by oxidation of D-glucose to gluconolactone |
| 1.1.1.12 | L-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 |
| 1.1.1.12 | L-arabinitol 4-dehydrogenase |
synthesis |
rare L-sugar L-xylulose is produced by the enzymatic oxidation of arabinitol to give a yield of approximately 86% |
| 1.1.1.133 | dTDP-4-dehydrorhamnose reductase |
synthesis |
development and evaluation of a modular system for large scale production of important dTDP-activated deoxyhexoses from dTMP and sucrose, overview |
| 1.1.1.133 | dTDP-4-dehydrorhamnose reductase |
synthesis |
six enzymes, including the dTDP-4-keto-rhamnose reductase, are involved in the pathway and are prepared by recombinant expression in Escherichia coli for large scale production of O-antigen precursor sTDP-L-rhamnose in a one-pot reaction, overview |
| 1.1.1.135 | GDP-6-deoxy-D-talose 4-dehydrogenase |
synthesis |
use of enzyme for synthesis of GDP-deoxyhexoses |
| 1.1.1.138 | mannitol 2-dehydrogenase (NADP+) |
synthesis |
commercial mannitol production as alternatives to less efficient chemical reduction of fructose |
| 1.1.1.138 | mannitol 2-dehydrogenase (NADP+) |
synthesis |
the enzyme of strain strain HH-01, KCCM-10252, is useful in production of D-mannitol |
| 1.1.1.14 | L-iditol 2-dehydrogenase |
synthesis |
L-sorbose is an important intermediate in the industrial vitamin C production process |
| 1.1.1.14 | L-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 |
| 1.1.1.140 | sorbitol-6-phosphate 2-dehydrogenase |
synthesis |
constitutive expression of the two sorbitol-6-phosphate dehydrogenase genes srlD1 and srlD2 in a mutant strain deficient for both L- and D-lactate dehydrogenase activities. Both Stl6PDH enzymes are active, and high specific activity can be detected in the overexpressing strains. Using resting cells under pH control with glucose as a substrate, both Stl6PDHs are capable of rerouting the glycolytic flux from fructose-6-phosphate toward sorbitol production with a remarkably high efficiency of 61 to 65% glucose conversion |
| 1.1.1.144 | perillyl-alcohol dehydrogenase |
synthesis |
expression of the genes for (-)-limonene synthase (SdLS), a limonene 7-hydroxylase (SdL7H, CYP71A76), a perillyl alcohol dehydrogenase (SdPOHDH) and perillic acid O-methyltransferase (SdPAOMT) in Nicotiana benthamiana in combination with a geranyl diphosphate synthase to boost precursor formation, results in production of methylperillate |
| 1.1.1.159 | 7alpha-hydroxysteroid dehydrogenase |
synthesis |
the enzyme is useful as biocatalyst in the reduction of 7-keto bile acids, co-operation with cholylglycine hydrolase, EC 3.5.1.24, overview |
| 1.1.1.159 | 7alpha-hydroxysteroid dehydrogenase |
synthesis |
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases |
| 1.1.1.16 | galactitol 2-dehydrogenase |
synthesis |
the enzyme can be used to produce optically pure building blocks and for the bioconversion of bioactive compounds |
| 1.1.1.16 | galactitol 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 |
| 1.1.1.17 | mannitol-1-phosphate 5-dehydrogenase |
synthesis |
strategy for mannitol production in Lactococcus, most promising is overexpression of enzyme in a lactate-dehydrogenase deficient strain |
| 1.1.1.17 | 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 |
| 1.1.1.175 | D-xylose 1-dehydrogenase |
synthesis |
expression of gene xylB in Saccharomyces cerevisiae results in production of 17 g D-xylonate/l at 0.23g/l/h from 23 g D-xylose/l. D-Xylonate accumulates intracellularly to 70 mg/g, xylitol to 18 mg/g. Cells expressing D-xylonolactone lactonase xylC from Caulobacter crescentus with xylB initially produce more extracellular D-xylonate than cells lacking xylC at both pH5.5 and pH3, and sustain higher production at pH3. Cell vitality and viability decreases during D-xylonate production at pH 3.0 |
| 1.1.1.176 | 12alpha-hydroxysteroid dehydrogenase |
synthesis |
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases |
| 1.1.1.179 | D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) |
synthesis |
production of up to19 g D-xylonate per litre in Kluyveromyces lactis expressing gene xyd1 upon growth on D-galactosel and D-xylose. D-Xylose uptake is not affected by deletion of either the D-xylose reductase XYL1 or a putative xylitol dehydrogenase encoding gene XYL2 in xyd1 expressing strains |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
enzyme is useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate, which is used in the synthesis of pharmacologically and biologically important compouds |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
enzyme might be useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate, which is used in the synthesis of pharmacologically and biologically important compounds |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
semienzymatic production of (R)-3-styrene oxide |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
the enzyme is useful for stereoselective enzymatic synthesis of chiral alcohols and chiral alcohol intermediates of pharmaceutical importance |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
production of carbonyl reductase by Candida viswanathii in 6.6 l fermentor, using controlled pH value at 8.0, aeration rate 1 vvm and an agitation speed of 250 rpm at 25°C. Use of enzyme for preparative scale reduction of N,N-dimethyl-3-keto-2-thienyl-propanamine to (S)-N,N-dimethyl-3-keto-2-thienyl-propanamine |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
production of Geotrichum candidum carbonyl reductase in a laboratory scale stirred tank bioreactor, optimization of conditions. At controlled pH value of 5.5 the specific enzyme activity is highest with 306 U/mg. Optimization of glucose concentration yields 21 g/l cell mass with 9770 U enzyme activity/g glucose |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
synthesis of (R)-beta-hydroxynitriles with good optical purity by use of recombinant carbonyl reductase and further conversion to (R)-beta-hydroxy carboxylic acids via a nitrilase-catalyzed hydrolysis |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
enzyme product ethyl (S)-4-chloro-3-hydroxybutanoate is a chiral compound valuable as a building block for pharmaceuticals |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
synthesis of (3S)-acetoin in a coupled system consisting of glucose dehydrogenase from Bacillus subtilis 168 and the NADPH-dependent carbonyl reductase. Under the optimal conditions, 12.2 g/l (3S)-acetoin is produced from 14.3 g/l diacetyl in 75 min |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98% |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
coexpression with glucose dehydrogenase from Bacillus subtilis for NADPH regeneration in Escherichia coli and optimization of linker peptides used for the fusion expression of carbonyl reductase and glucose dehydrogenase. Up to 297.3 g/L (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol with enantiopurity >99.9% ee is produced via reduction of 1.2 M of substrate with a 96.7% yield and productivity of 29.7 g/(L h) |
| 1.1.1.184 | carbonyl reductase (NADPH) |
synthesis |
in situ expression in Candida leads to over fourfold higher activity for conversion of racemic (R,S)-1-phenyl-1,2-ethanediol to 2-hydroxyacetophenone, while maintaining the activity for catalyzing 2-hydroxyacetophenone to (S)-1-phenyl-1,2-ethanediol. A recombinant Candida parapsilosis converts racemic (R,S)-1-phenyl-1,2-ethanediol to its (S)-isomer with an optical purity of 98.8% and a yield of 48.4%. The biotransformation duration is reduced from 48 to 13 h |
| 1.1.1.188 | prostaglandin-F synthase |
synthesis |
development of a coupled assay method for enzymatic formation of prostamide F2alpha from anandamide by the cyclooxygenase-II and the prostaglandin synthase F involving the intermediate metabolite, prostamide H2 |
| 1.1.1.194 | coniferyl-alcohol dehydrogenase |
synthesis |
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol |
| 1.1.1.195 | cinnamyl-alcohol dehydrogenase |
synthesis |
synthesis of cinnamyl alcohol from cinnamaldehyde using the isolated enzyme or by expression of enzyme in Escherichia coli. The reduction of cinnamaldehyde by the isolated enzyme occurrs in 3 h at 50°C with 97% conversion, and yields high purity cinnamyl alcohol with a yield of 88% and a productivity of 50 g/g enzyme. The reduction of 12.5 g/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 |
| 1.1.1.195 | cinnamyl-alcohol dehydrogenase |
synthesis |
potential exploitation of rationally engineered forms of CAD2 for the targeted modification of monolignol composition in transgenic plants |
| 1.1.1.198 | (+)-borneol dehydrogenase |
synthesis |
production of enzyme in the form of inclusion body in Escherichia coli. The refolded BDH1 tends to precipitate. Insoluble recombinant BDH1 is converted into a soluble form by adding glycerol in LB medium |
| 1.1.1.198 | (+)-borneol dehydrogenase |
synthesis |
recombinant borneol dehydrogenase is found in inclusion bodies when expressed in Escherichia coli. Changing the medium from lysogeny broth to Terrific Broth yield a soluble form of the enzyme |
| 1.1.1.2 | alcohol dehydrogenase (NADP+) |
synthesis |
- |
| 1.1.1.2 | 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 |
| 1.1.1.2 | 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 |
| 1.1.1.2 | alcohol dehydrogenase (NADP+) |
synthesis |
reduction of industrially important compounds cinnamyl aldehyde and anisaldehyde, industrial bioconversion of useful alcohols and aldehydes |
| 1.1.1.2 | alcohol dehydrogenase (NADP+) |
synthesis |
useful for asymmetric production of L-carnitine |
| 1.1.1.2 | alcohol dehydrogenase (NADP+) |
synthesis |
industrial ethanol production |
| 1.1.1.2 | 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 |
| 1.1.1.2 | 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 |
| 1.1.1.2 | 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 |
| 1.1.1.2 | 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 |
| 1.1.1.2 | 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 |
| 1.1.1.2 | 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 |
| 1.1.1.2 | alcohol dehydrogenase (NADP+) |
synthesis |
engineering ADHs for regenerating NADPH by oxidation of diols |
