EC Number   |
Recommended Name |
Application |
|---|
    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.B18 | 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 |
| 1.1.1.B19 | 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 |
| 1.1.1.B19 | xylitol dehydrogenase (NAD+) |
synthesis |
enzyme XDH from Erwinia aphidicola can be useful for production of L-xylulose, a rare ketose, for apllication in pharmaceutical and food industries |
| 1.1.1.B20 | meso-2,3-butandiol dehydrogenase |
synthesis |
discovery of the (S)-selective alcohol dehydrogenase enables a novel production process of (R)-acetoin from meso-2,3-butanediol |
| 1.1.1.B20 | meso-2,3-butandiol dehydrogenase |
synthesis |
Bacillus licheniformis strain MW3 (DELTAbudCDELTAgdh) can be useful for the production of acetoin on a commercial scale |
| 1.1.1.B20 | meso-2,3-butandiol dehydrogenase |
synthesis |
Bacillus subtilis enzyme BS-BDH is a potential candidate for L-(+)-acetoin production |
| 1.1.1.B20 | meso-2,3-butandiol dehydrogenase |
synthesis |
Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO) and can be utilized for large scale production |
| 1.1.1.21 | aldose 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 |
| 1.1.1.22 | UDP-glucose 6-dehydrogenase |
synthesis |
the high activity combined with the simple purification procedure used make GbUGD a valuable alternative biocatalyst for the synthesis of UDP-glucuronic acid or the development of NAD+ regeneration systems |
| 1.1.1.22 | UDP-glucose 6-dehydrogenase |
synthesis |
use of recombinant Triton-permeabilized cells of Schizosaccharomyces pombe to synthesize UDP-glucuronic acid with 100 % yield and selectivity. 5 mM UDP-glucose are converted into 5 mM UDP-glucuronic acid within 3 h |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
development of yeast-based bioprocesses to produce lactate from lignocellulosic raw material |
| 1.1.1.27 | 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 |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
the enzyme might be useful in the production of phenyllactate |
| 1.1.1.27 | 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 |
| 1.1.1.27 | 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 |
| 1.1.1.27 | 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 |
| 1.1.1.27 | 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 |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
L-nLDH is an efficient catalyst that can be used in the enantioselective reduction of alpha-keto acids to alpha-hydroxy acids |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
coexpression of enzyme and glucose dehydrogenase gene in Escherichia coli efficiently reduces 3,4-dihydroxyphenylpyruvate to L-3,4-dihydroxyphenyllactate with 95.45% isolation yield |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain co-expressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3 |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain coexpressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3 |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
production of phenyllactic acid from L-Phe by recombinant Escherichia coli coexpressing L-phenylalanine oxidase and L-lactate dehydrogenase. At optimal conditions (L-Phe 6 g/l, pH 7.5, 35°C, CDW 24.5 g/l and 200 rpm), the recombinant strain produces 1.62 g L-phenylalanine/l with a conversion of 28% from L-Phe |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
production of (R)-2-hydroxy-4-phenyl-butyric acid, which is a precursor for different ACE-inhibitors |
| 1.1.1.28 | 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 |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
D-LDH is a candidate for thermophilic D-lactic acid production |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
the polymers of lactic acid are used as biodegradable bioplastics. Polylactic acid, biodegradable polyester polymer of lactic acid, is mainly produced through a bacterial fermentation process |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
the recombinant enzyme from Pediococcus pentosaceus can be used for production of 3-phenyllactic acid (2-hydroxy-3-phenylpropanoic acid, PLA), an antimicrobial compound with broad spectrum activity against both bacteria and fungi, optimization by coexpression of Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2, for NADH regeneration |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
asymmetric synthesis of (R)-2-hydroxy-4-phenylbutyric acid using recombinant Pichia pastoris expressing the Tyr52Leu variant of D-lactate dehydrogenase from Lactobacillus plantarum. The recombinant yeast cells show catalytic activity at a high concentration of 2-oxo-4-phenylbutyric acid (380 mM, 76 g/l). Under optimized reaction conditions (pH 7.5, 37°C, and 2% glucose), a full conversion with over 95% reaction yield and about 100% product enantiomeric excess is achieved |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
recombinant Escherichia coli expressing D-lactate dehydrogenase, without coexpression of a cofactor regeneration system, can produce 20.5 g/l D-phenyllactic acid with enantiomeric excess above 99% from phenylpyruvic acid in a fed-batch biotransformation process, with a productivity of 49.2 g/l per day |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
recombinant Escherichia coli expressing Ldb0101 achieves a D-lactate concentration of 949.6 mg/l under aerobic and 1.94 g/l under anaerobic conditions, respectively |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
recombinant Escherichia coli expressing Ldb1010 achieves a D-lactate concentration of 850 mg/l |
| 1.1.1.28 | D-lactate dehydrogenase |
synthesis |
synthesis of D-phenyllactic acid by Escherichia coli expressing D-lactate dehdrogenase plus Exiguobacterium sibiricum glucose dehydrogenase. The total enzyme activity in the fermentation broth reaches 2359.0 U/l when induced by 10 g/l lactose at 28°C and 150 rpm for 14 h. Under the optimized biocatalysis conditions, 50 g/l sodium phenylpyruvate is completely converted to D-phenyllactic acid with a space-time yield and enantiomeric excess of 262.8 g/l day and over 99.5%, respectively |
| 1.1.1.30 | 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 |
| 1.1.1.35 | 3-hydroxyacyl-CoA dehydrogenase |
synthesis |
the enzyme is used in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to (S)-3-hydroxybutyryl-CoA |
| 1.1.1.35 | 3-hydroxyacyl-CoA dehydrogenase |
synthesis |
the highly efficient mutant enzyme K50A/K54A/L232Y can be useful for increasing the production rate of n-butanol |
| 1.1.1.36 | acetoacetyl-CoA reductase |
synthesis |
PHB-synthesis for thermoplastics |
| 1.1.1.36 | 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 |
| 1.1.1.36 | acetoacetyl-CoA reductase |
synthesis |
the engineered enzyme mutant T173S can be used for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system |
| 1.1.1.39 | 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 |
| 1.1.1.44 | phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) |
synthesis |
thermostability may lead to some practical applications |
| 1.1.1.44 | phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) |
synthesis |
NADPH regeneration. When coupled with glucose-6-phosphate dehydrogenase the enzyme generates two moles of NADPH per mole of glucose-6-phosphate |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
synthesis |
enzyme can be used for gluconic acid production in low water systems |
| 1.1.1.47 | 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 |
| 1.1.1.47 | 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 |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
synthesis |
(±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
synthesis |
co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
synthesis |
glucose dehydrogenase is a general tool for driving nicotinamide (NAD(P)H) regeneration in synthetic biochemistry. Coupled with a Candida glabrata carbonyl reductase, the mutant glucose dehydrogenase Q252L/E170K/S100P/K166R/V72I/K137R is successfully used for the asymmetric reduction of deactivating ethyl 2-oxo-4-phenylbutyrate with total turnover number of 1800 for the nicotinamide cofactor, thus making it attractive for commercial application |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
synthesis |
production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, an important chiral intermediate for the synthesis of rosuvastatin, using carbonyl reductase coupled with glucose dehydrogenase. A recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase is constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant Escherichia coli cells are applied for the efficient production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess of more than 99.0% under 350 g/l of tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate after 12 h reaction. A substrate fed-batch strategy is further employed to increase the substrate concentration to 400 g/l resulting in an enhanced product yield to 98.5% after 12 h reaction in a 1 l bioreactor. Meanwhile, the space-time yield is 1182.3 g/l*day |
| 1.1.1.49 | glucose-6-phosphate dehydrogenase (NADP+) |
synthesis |
bacitracin, a kind of cyclic peptide antibiotic mainly produced by Bacillus, has wide ranges of applications. The bacitracin production is enhanced by by NADPH generation via overexpressing glucose-6-phosphate dehydrogenase Zwf in Bacillus licheniformis |
| 1.1.1.50 | 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 |
| 1.1.1.50 | 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) |
synthesis |
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 |
| 1.1.1.51 | 3(or 17)beta-hydroxysteroid dehydrogenase |
synthesis |
engineering Mycobacterium smegmatis for testosterone production. Mycobacterium smegmatis is an excellent chassis to develop biotechnological processes for the biotransformation of sterols and their derivatives into valuable pharmaceutical compounds. Overexpression of the gene encoding microbial 17beta-hydroxysteroid: NADP 17-oxidoreductase, from the bacterium Comamonas testosteroni. The host strains are Mycobacterium smegmatis wild type and a genetic engineered androst-4-ene-3,17-dione producing mutant. The recombinant strains are able to produce testosterone from androst-4-ene-3,17-dione and/or from sterols with high yields |
| 1.1.1.51 | 3(or 17)beta-hydroxysteroid dehydrogenase |
synthesis |
engineering Mycobacterium smegmatis for testosterone production. Mycobacterium smegmatis is an excellent chassis to develop biotechnological processes for the biotransformation of sterols and their derivatives into valuable pharmaceutical compounds. Overexpression of the gene encoding microbial 17beta-hydroxysteroid: NADP 17-oxidoreductase, from the fungus Cochliobolus lunatus. The host strains are Mycobacterium smegmatis wild type and a genetic engineered androst-4-ene-3,17-dione producing mutant. The recombinant strains are able to produce testosterone from androst-4-ene-3,17-dione and/or from sterols with high yields |
| 1.1.1.B51 | 3-quinuclidinone reductase (NADPH) |
synthesis |
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals |
| 1.1.1.B51 | 3-quinuclidinone reductase (NADPH) |
synthesis |
the enzyme can be used for synthesis of optically pure 3-quinuclidinol. Optically pure 3-quinuclidinol is an important intermediate for the synthesis of various anticholinergic drugs. (R)-3-Quinuclidinol is used to synthesize muscarinic M1 or M3 receptor antagonists such as talsaclidine, revatropate, and solifenacin |
| 1.1.1.B52 | 3-quinuclidinone reductase (NADH) |
synthesis |
stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals |
| 1.1.1.B52 | 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 |
| 1.1.1.B52 | 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% |
| 1.1.1.B52 | 3-quinuclidinone reductase (NADH) |
synthesis |
(R)-3-quinuclidinol is a valuable intermediate for pharmaceuticals. The enzyme can be used for the synthesis of the enantiopure compound |
| 1.1.1.56 | ribitol 2-dehydrogenase |
synthesis |
the recombinant Escherichia coli expressing D-psicose-3-epimerase (DPE), ribitol dehydrogenase (RDH) and formate dehydrogenase (FDH) is constructed and used together with immobilized GI for allitol bioproduction from D-glucose. The conditions of allitol biotransformation, the cell catalytic activity resistance, the cell cultivation medium, and fed-batch culture conditions are optimized |
| 1.1.1.58 | 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 |
| 1.1.1.B60 | D-sorbitol dehydrogenase (NADP+) |
synthesis |
synthesis of L-sorbose is largely used as a starting material for L-ascorbic acid biosynthesis. It can been also used to synthesize the potent glycosidase inhibitor 1-deoxygalactonojirim and rare sugars such as L-tagatose and L-iditol. Escherichia coli(gosldh-lrenox) producing both GoSLDH for D-sorbitol oxidation and LreNOX (NAD(P)H oxidase from Lactobacillus reuteri) for NADP+ regeneration is generated and used for L-sorbose production. L-Sorbose production by Escherichi coli(gosldh-lrenox) reaches 4.1 g/l after 40 min, which was 20.5fold higher than that of Escherichia coli(gosldh). This system reduces the NADPH inhibition effect in the GoSLDH reaction and enables high production of L-sorbose from D-sorbitol |
| 1.1.1.B63 | 3-quinuclidinone reductase (NADP+) |
synthesis |
the enzyme can be used for synthesis of optically pure 3-quinuclidinol. Optically pure 3-quinuclidinol is an important intermediate for the synthesis of various anticholinergic drugs. (S)-3-Quinuclidinol is a very promising chiral building blocks for synthesis of serotonin receptor antagonist drugs and anticholinergic drugs |
| 1.1.1.67 | mannitol 2-dehydrogenase |
synthesis |
the recombinant enzyme expressed in Bacillus megaterium is useful in production of D-mannitol using a resting cell biotransformation approach |
| 1.1.1.67 | mannitol 2-dehydrogenase |
synthesis |
an effective strategy for producing high yields of mannitol is developed. The combined strategies of aeration induction and redox modulation significantly increases the glucose consumption rate, intracellular NADH level and the specific activity of mannitol dehydrogenase (MDH), resulting in an increase in mannitol production from 64.6 to 88.1 g/l with the yield increased from 0.69 to 0.94 g/g |
| 1.1.1.67 | mannitol 2-dehydrogenase |
synthesis |
mannitol is a natural hexitol with important applications in medicine and food industry. Development of a production method on an industrial scale, optimization and evaluation of production in a batch reactor (BR, or BRP operation) for a complex bi-enzymatic system with suspended enzymes and cofactor regeneration, method modeling, molecular calculations and simulations, detailed overview |
| 1.1.1.67 | mannitol 2-dehydrogenase |
synthesis |
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga maritima involves production from glucose via Thermotoga neapolitana xylose isomerase (gene xylA, UniProt ID P45687) followed by the conversion of the formed D-fructose using Thermotoga maritima MtDH of enzymatic to chemical synthesis process, overview |
| 1.1.1.67 | mannitol 2-dehydrogenase |
synthesis |
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga neapolitana is via D-fructose in a single step procedure. Comparison of enzymatic to chemical synthesis process, overview |
| 1.1.1.69 | gluconate 5-dehydrogenase |
synthesis |
strain overexpressing enzyme plus Escherichia coli transhydrogenase sthA, enhanced accumulation of 5-ketoD-gluconate, precursor of L-(+)-tartaric acid |
| 1.1.1.76 | (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 |
| 1.1.1.76 | (S,S)-butanediol dehydrogenase |
synthesis |
the key enzymes in the microbial production of 2,3-butanediol |
| 1.1.1.77 | lactaldehyde reductase |
synthesis |
fermentation of L-rhamnose, L-fucose and D-fucose to a mixture of 1,2-propanediol, acetone, H2, CO2 and ethanol |
| 1.1.1.81 | hydroxypyruvate reductase |
synthesis |
potential application in the enzymatic synthesis of glyoxylate |
| 1.1.1.87 | homoisocitrate dehydrogenase |
synthesis |
novel glutarate biosynthetic pathway by incorporation of a +1 carbon chain extension pathway from 2-oxoglutarate in combination with 2-oxo acid decarboxylation pathway in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD). The recombinant Escherichia coli coexpressing all five genes produces 0.3 g/l glutarate from glucose. To further improve the titers, 2-oxoglutarate is rechanneled into carbon chain extension pathway via the clustered regularly interspersed palindromic repeats system mediated interference (CRISPRi) of essential genes sucA and sucB in tricarboxylic acid cycle. The final strain can produce 0.42 g/l glutarate, which is increased by 40% compared with the parental strain. Glutarate is one of the most potential building blocks for bioplastics |
| 1.1.1.90 | aryl-alcohol dehydrogenase |
synthesis |
biotechnological production of vanillin |
| 1.1.1.94 | glycerol-3-phosphate dehydrogenase [NAD(P)+] |
synthesis |
development of a whole-cell biocatalyst for NAD(P)H cofactor regeneration that employs permeabilized Escherichia coli cells in which the glpD and gldA genes are deleted and the gpsA gene is overexpressed. The biocatalyst involves an economical substrate, bifunctional regeneration of NAD(P)H, and simple reaction conditions as well as a stable environment for enzymes, and is applicable to a variety of oxidoreductase reactions requiring NAD(P)H regeneration |
| 1.1.1.95 | phosphoglycerate dehydrogenase |
synthesis |
metabolic engineering of Corynebacterium glutamicum for L-serine production by enzyme overexpression |
| 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 |
| 1.1.1.133 | 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 |
| 1.1.1.140 | 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 |
| 1.1.1.175 | 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 |
