EC Number   |
Recommended Name |
Application |
|---|
  4.4.1.32 | C-phycocyanin alpha-cysteine-84 phycocyanobilin lyase |
synthesis |
production of of a fluorescent holo-C-phycocyanin subunit alpha in Escherichia coli by construction of an expression vector containing five essential genes in charge of biosynthesis of cyanobacterial C-phycocyanin holo-alpha subunit. The vector harbors two cassettes: one cassette carries genes hox1 and pcyA required for conversion of heme to phycocyanobilin, and the other cassette carries cpcA encoding C-phycocyanin subunit alpha along with lyase subunits cpcE and cpcF both of which are necessary and sufficient for the correct addition of phycobiliprotein to CpcA. The maximum peak of absorbance spectrum is at 623 nm, and the maximum peak of fluorescence emission and excitation are at 648 and 633 nm, respectively, which are similar to those of native C-phycocyanin |
 4.2.2.14 | glucuronan lyase |
synthesis |
production of oligoglucuronans by enzymatic depolymerization of nascent glucuronan |
 3.8.1.2 | (S)-2-haloacid dehalogenase |
synthesis |
production of optically active 2-hydroxyalkanoic acids and 2-haloalkanoic acids for chiral synthesis in industry |
| 1.14.14.11 | styrene monooxygenase |
synthesis |
production of optically pure (S)-styrene oxide, an important building block in organic synthesis. Recombinant Escherichia coli producing styrene monooxygenase catalyzes the formation of (S)-2-phenyloxirane from inexpensive styrene with an excellent enantiomeric excess of more than 99% at rates up to 180 U/g (dry weight) of cells |
| 1.14.13.22 | cyclohexanone monooxygenase |
synthesis |
production of optically pure sulfoxides by biotransformation in whole cell systems of several sulfides, dithianes and dithiolanes |
| 4.1.2.46 | aliphatic (R)-hydroxynitrile lyase |
synthesis |
production of organosilicon compounds by enantioselective transcyanation. Under optimum conditions, both acetyltrimethylsilane conversion to (R)-2-trimethylsilyl-2-hydroxy-ethylcyanide and enantiomeric excess of the product are above 99%. the silicon atom in acetyltrimethylsilane has a great effect on the eaction and both the substrate conversion and the product enantiomeric excess are much higher than those in its carbon counterpart 3,3-dimethyl-2-butanone |
| 5.4.99.11 | isomaltulose synthase |
synthesis |
production of palatinose, which is used as a sweetener and as a substitute for sucrose |
| 3.1.1.25 | 1,4-lactonase |
synthesis |
production of pantoic acid, which is used as a Vitamin B2-complex, production of D- and L-pantolactones, which are used as chiral intermediates in chemical synthesis |
| 4.2.2.10 | pectin lyase |
synthesis |
production of pectin lyase by Aspergillus giganteus. The highest activity, using citrus pectin as carbon source, is obtained in 11-day-old standing cultures, but the highest specific activity is obtained in 6.5-day-old shaken cultures, at pH 6.5 and 35°C. Using orange waste as carbon source, the highest activity is observed in 8-day-old standing cultures, at pH 7.0 and 30°C |
| 4.2.3.7 | pentalenene synthase |
synthesis |
production of pentalenene by expression of pentalenene synthase gene in Xanthophyllomyces dendrorhous with concurrent knock out of the native crtE or crtYB genes. Culturing the yeast in presence of dodecane traps the volatile compounds produced, and no other terpenoids are found as by products |
| 5.1.1.11 | phenylalanine racemase (ATP-hydrolysing) |
synthesis |
production of phenylalanine racemase in continuous culture |
| 3.4.21.62 | Subtilisin |
synthesis |
production of phenylalanine, which is used as an intermediate for the synthesis of aspartame |
| 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 |
| 4.3.1.19 | threonine ammonia-lyase |
synthesis |
production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) from a single unrelated carbon source via threonine biosynthesis in Escherichia coli, by overexpression of threonine deaminase, which is the key factor for providing propionyl-coenzyme A (propionyl-CoA), from different host bacteria, removal of the feedback inhibition of threonine by mutating and overexpressing the thrABC operon in Escherichia coli, and knock-out of the competitive pathways of catalytic conversion of propionyl-CoA to 3-hydroxyvaleryl-CoA. Construction of a series of strains and mutants leads to production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer with differing monomer compositions in a modified M9 medium supplemented with 20 g/liter xylose. The largest 3-hydroxyvalerate fraction obtained in the copolymer is 17.5 mol% |
| 3.4.11.1 | leucyl aminopeptidase |
synthesis |
production of polyketide antibiotics |
| 5.1.99.1 | methylmalonyl-CoA epimerase |
synthesis |
production of polyketides like myxothiazol requiring methylmalonyl-CoA as an extender unit |
| 4.2.1.84 | nitrile hydratase |
synthesis |
production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h |
| 3.1.1.20 | tannase |
synthesis |
production of propyl gallate for the food industry and trimethoprim in the pharmaceutical industry |
| 1.1.99.30 | 2-oxo-acid reductase |
synthesis |
production of pyruvate from (R)-lactate in an enzyme-membrane reactor with coupled electrochemical regeneration of the artificial mediator anthraquinone-2,6-disulfonate |
| 1.1.99.6 | D-lactate dehydrogenase (acceptor) |
synthesis |
production of pyruvate in an enzyme-membrane reactor |
| 1.2.4.1 | pyruvate dehydrogenase (acetyl-transferring) |
synthesis |
production of pyruvate in an Escherichia coli strain with central metabolic pathways modified. Genes ldhA, pflB, pta-ackA, poxB, ppc, frdBC are knocked out sequentially and full pyruvate dehydrogenase is retained. In batch fermentation with M9 medium, pyruvate yield and production rate reach 0.63 g/g glucose and 1.89 g/(1 h), respectively. The production of acetate, succinate, and other carboxylates is effectively controlled, while the pathways of convertion of pyruvate to phosphoenol pyruvate and acetyl CoA are enhanced |
| 2.5.1.72 | quinolinate synthase |
synthesis |
production of quinolinic acid from L-aspartate, dihydroxyacetone phosphate, and O2 by use of enzymes NadA and NadB |
| 2.4.1.276 | zeaxanthin glucosyltransferase |
synthesis |
production of rare beta-carotene-modified carotenoids possessing 2-O, 2-H or 2-glucosyl and/or 3-O, 3-H or 3-glucosyl functionalities in their beta-ionone rings using a recombinant Escherichia coli approach, involving expression of carotenoid biosynthesis genes crtE, crtB, crtI, crtY, crtZ, crtX and crtG. From the cells of the recombinant Escherichia coli, caloxanthin i.e. (beta,beta-carotene-2,3,2',3'-tetrol)-3'-beta-D-glucose, zeaxanthin i.e. (beta,beta-carotene-3,3'-diol) 3,3'-beta-D-diglucoside, and nostoxanthin i.e. (beta,beta-carotene-2,3,3'-triol) are isolated and identified. Caloxanthin 3'-beta-D-glucoside displays potent 1O2 quenching activity |
| 1.11.1.6 | catalase |
synthesis |
production of recombinant Bacillus subtilis catalase and purification from culture fluid. Purified enzyme has a specific activity of 34600 U/mg and is more resistant to acidic conditions than bovine liver catalase |
| 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 |
| 3.4.21.5 | thrombin |
synthesis |
production of recombinant human prethrombin-2 in mouse myeloma cells, activation by recombinant ecarin and purification by affinity chromatography. Yield is about 70%, product is indistinguishable from plasma-derived enzyme |
| 1.1.99.35 | soluble quinoprotein glucose dehydrogenase |
synthesis |
production of recombinant soluble isoform by expression in Klebsiella pneumoniae at about 18 000 U per l, equal to that achieved in recombinant Escherichia coli. The signal sequence of recombinant PQQGDH-B produced by Klebsiella pneumoniae is correctly processed |
| 1.13.11.63 | beta-carotene 15,15'-dioxygenase |
synthesis |
production of retinal from beta-carotene using recombinant enzyme. The optimum pH, temperature, substrate and detergent concentrations, and enzyme amount for effective retinal production are 9.0, 37°C, 200 mg per ml beta-carotene, 5% w/v Tween 40, and 0.2 U per ml enzyme, respectively. Under optimum conditions, the recombinant enzyme produces 72 mg per ml retinal in a 15 h reaction time, with a conversion yield of 36% w/w |
| 2.4.2.2 | pyrimidine-nucleoside phosphorylase |
synthesis |
production of ribavirin, which is an antiviral drug |
| 5.3.1.4 | L-arabinose isomerase |
synthesis |
production of ribose by immobilized recombinant Escherichia coli cells expressing the L-arabinose isomerase gene and mannose-6-phosphate isomerase mutant W17Q/N90A/L129F. The immobilized cells produce 99 g/l L-ribose from 300 g/l L-arabinose in 3 h at pH 7.5 and 60 °C in the presence of 1 mM Co2+, with a conversion yield of 33 % (w/w) and a productivity of 33 g/l/h |
| 5.3.1.8 | mannose-6-phosphate isomerase |
synthesis |
production of ribose by immobilized recombinant Escherichia coli cells expressing the L-arabinose isomerase gene and mannose-6-phosphate isomerase mutant W17Q/N90A/L129F. The immobilized cells produce 99 g/l L-ribose from 300 g/l L-arabinose in 3 h at pH 7.5 and 60°C in the presence of 1 mM Co2+, with a conversion yield of 33% (w/w) and a productivity of 33 g/l/h |
| 2.3.1.140 | rosmarinate synthase |
synthesis |
production of rosmarinic acid analogues in Escherichia coli by expression of 4-coumarate: CoA ligase from Arabidopsis thaliana and rosmarinic acid synthase from Coleus blumei. Incubation of the recombinant strain with exogenously supplied phenyllactic acid and analogues, and coumaric acid and analogues as donor substrates leads to production of 18 compounds, including unnatural analogues |
| 2.1.1.232 | naringenin 7-O-methyltransferase |
synthesis |
production of sakuranetin (7-O-methylnaringenin) and ponciretin (4-O-methylnaringenin) in Escherichia coli by reconstruction of the naringenin biosynthesis pathway. Engineering the shikimic acid pathway, and overexpression of several genes for the biosynthesis of ponciretin and sakuranetin such as tyrosine ammonia lyase, 4-coumaroyl CoA ligase, chalcone synthase, and O-methyltransferase and deletion of isocitrate dehydrogenase finally gives ponciretin and sakuranetin from glucose in Escherichia coli at the concentration of 42.5 mg/l and 40.1 mg/l, respectively |
| 3.2.1.17 | lysozyme |
synthesis |
production of secreted recombinant human lysozyme by use of overexpression vector pPIC3.5k, carrying the strong promoter AOX1 of aldehyde oxidase 1, the HSA signal peptide, the enterokinase recognition motif, and the lysozyme gene. Mature protein is identical with native human lysozyme. It exhibits in vitro bacteriolytic activity against the Gram-positive bacterium Micrococcus lysodeikticus and the Gram-negative bacterium Escherichia coli |
| 2.4.1.389 | solabiose phosphorylase |
synthesis |
production of solabiose from lactose and sucrose. Lactose is hydrolyzed to D-galactose and D-glucose by beta-galactosidase. Phosphorolysis of sucrose and synthesis of solabiose are then coupled by adding sucrose, sucrose phosphorylase, and enzyme PBOR_28850 to the reaction mixture. Using 210 mmol lactose and 280 mmol sucrose, 207 mmol of solabiose is produced. Yeast treatment degrades the remaining monosaccharides and sucrose without reducing solabiose. Solabiose with a purity of 93.7% is obtained without any chromatographic procedures |
| 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 |
| 4.1.1.63 | protocatechuate decarboxylase |
synthesis |
production of the 4-hydroxybenzoate, protocatechuate, and catechol in Escherichia coli. To enhance endogenous biosynthesis of 4-hydroxybenzoate, native chorismate pyruvate lyase ubiC is overexpressed. 4-Hydroxybenzoate is converted to protocatechuate by hydroxylase pobA from Pseudomonas aeruginosa. Catechol is produced by the additional coexpression of protocatechuate decarboxylase from Enterobacter cloacae. Systematic expression of appropriate pathway elements in phenylalanine overproducing Escherichia coli enables initial titers of 32, 110, and 81 mg/l for 4-hydroxybenzoate, protocatechuate, and catechol, respectively. Disruption of chorismate mutase/prephenate dehydratase (pheA) to preserve endogenous chorismate then allows maximum titers of 277, 454, and 451 mg/l, respectively, at glucose yields of 5.8, 9.7, and 14.3% of their respective theoretical maxima |
| 2.4.1.10 | levansucrase |
synthesis |
production of the artificial sweetener, lactosucrose |
| 2.1.1.128 | (RS)-norcoclaurine 6-O-methyltransferase |
synthesis |
production of the economically important analgesic morphine and the antimicrobial agent berberine |
| 1.2.1.104 | pyruvate dehydrogenase system |
synthesis |
production of the functional pyruvate dehydrogenase complex. All components are coexpressed in the cytoplasm of baculovirus-infected SF9 cells by deletion of the mitochondrial localization signal sequences and E1a is FLAG-tagged to facilitate purification. The protein complex is purified using FLAG-M2 affinity resin, followed by Superdex 200 sizing chromatography. The E2 and E3BP components are then lipoylated in vitro. The resulting complex is over 90% pure and homogenous |
| 5.3.1.4 | L-arabinose isomerase |
synthesis |
production of the intracellular enzymes L-arabinose isomerase and D-xylose isomerase in Lactobacillus bifermentans. After 9 h cultivation in optimized medium, Arabinose isomerase and xylose isomerase activities are 9.4 and 7.24 U/ml, respectively. For optimal growth, the strain requires Tween 80 at 1 g/l and a source of inorganic nitrogen, e.g., ammonium citrate. The bacterium has no requirement for sodium acetate for either growth or production of isomerases. The production rate of enzymes is increased when metal ions are added, primarily manganese |
| 1.11.1.16 | versatile peroxidase |
synthesis |
production of the oxidase in strain BL21(DE3)pLysS, cultivated at 25°C in auto-induction medium and presence of heme |
| 3.2.1.193 | ginsenosidase type I |
synthesis |
production of the pharmacologically active minor ginsenoside F2 from the major ginsenosides Rb1 and Rd by using the recombinant Lactococcus lactis strain expressing heterologous the beta-glucosidase gene |
| 5.2.1.5 | linoleate isomerase |
synthesis |
production of trans-10,cis-12-linoleic acid as a single isomer by expression of a fusion construct with enhanced green fluorescent protein on the surface of yeast cells. Upon optimization, a maximum yield of trans-10,cis-12-linoleic acid of 4 mg/ml is observed within 20 h using the strain as whole-cell biocatalyst |
| 5.2.1.5 | linoleate isomerase |
synthesis |
production of trans-10,cis-12-linoleic acid by codon-optimized expression in Mortierella alpina. In presence of 5 microM long-chain acyl-CoA synthetase inhibitor the trans-10,cis-12-linoleic acid content reaches up to 29 mg/l |
| 5.4.99.15 | (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase |
synthesis |
production of trehalose by enzyme plus maltooligosyltrehalose trehalohydrolase is increased in presence of 4-alpha-glucanotransferase, converting 70% of maltopentaose into trehalose after 6 h, while 60% is converted without 4-alpha-glucanotransferase |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
synthesis |
production of trehalose from starch |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
synthesis |
production of trehalose from starch. Trehalose is utilized as a stabilizer for dried or frozen food, in cosmetics and in medicines as a drug additive |
| 6.3.1.9 | trypanothione synthase |
synthesis |
production of trypanothione and trypanothione disulfide in >200 mg quantities by mutant C59A lacking the amidase activity. The protocol also allows the synthesis of related glutathione conjugates |
| 5.4.99.17 | squalene-hopene cyclase |
synthesis |
production of unnatural polyprenoids and supranatural steroids by manipulation of the enzyme reaction by combination of substrate analogues |
| 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 |
| 1.3.99.17 | quinoline 2-oxidoreductase |
synthesis |
production of uracil in supernatant of resting cells with a yield of more than 98% |
| 5.4.99.9 | UDP-galactopyranose mutase |
synthesis |
production of uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactofuranosyl ester, a precursor required for the formation of the lipopolysaccharide O-antigen of Klebsiella pneumoniae serotype O1 |
| 1.14.14.108 | 2,5-diketocamphane 1,2-monooxygenase |
synthesis |
production of useful chiral synthons for chemoenzymatic synthesis |
| 1.14.14.155 | 3,6-diketocamphane 1,2-monooxygenase |
synthesis |
production of useful chiral synthons for chemoenzymatic synthesis |
| 4.2.1.118 | 3-dehydroshikimate dehydratase |
synthesis |
production of vanillin by engineered pathway in Schizosaccharomyces pombe or Saccharomyces cerevisiae. Pathway involves incorporation of 3-dehydroshikimate dehydratase, an aromatic carboxylic acid reductase from a bacterium of the Nocardia genus, and an O-ethyltransferase from Homo sapiens. In Saccharomyces cerevisiae, the aromatic carboxylic acid reductase enzyme requires activation by phosphopantetheinylation, achieved by coexpression of a Corynebacterium glutamicum phosphopantetheinyl transferase. Prevention of reduction of vanillin to vanillyl alcohol is achieved by knockout of the host alcohol dehydrogenase ADH6. In Schizosaccharomyces pombe, the biosynthesis is further improved by introduction of an Arabidopsis thaliana family 1 UDPglycosyltransferase, converting vanillin into vanillin beta-D-glucoside, which is not toxic to the yeast cells and thus may be accumulated in larger amounts |
| 1.1.1.307 | D-xylose reductase [NAD(P)H] |
synthesis |
production of xylitol |
| 3.1.1.110 | xylono-1,5-lactonase |
synthesis |
production of xylonate from xylose in Escerichia coli. Through the coexpression of a xylose dehydrogenase (XdH) and a xylonolactonase (XylC) from Caulobacter crescentus, the recombinant strain can convert 1 g/l xylose to 0.84 g/l xylonate and 0.10 g/l xylonolactone. After disruption of endogenous genes XylA and XylB encoding xylose isomerase and xylulose kinase, the finally engineered strain under fed-batch conditions, produces up to 27.3 g/l xylonate and 1.7 g/l xylonolactone from 30 g/l xylose, about 88% of the theoretical yield |
| 6.3.4.15 | biotin-[biotin carboxyl-carrier protein] ligase |
synthesis |
production of [35S]-biotin from Na-35SO4 and desthiobiotin with a specific activity of 30.7 Ci/mmol by expression of the biotinylation domain from the Plasmodium falciparum acetyl-CoA carboxylase in Escherichia coli as a biotinylation substrate. Overexpression of the biotin synthase, BioB, and biotin ligase, BirA, increases biotinylation of the biotinylation domain 160fold over basal levels. Biotinylated biotinylation domain is purified by affinity chromatography, and free biotin is liberated using acid hydrolysis |
| 3.1.1.3 | triacylglycerol lipase |
synthesis |
production of [4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one acetate, which is a hydroxymethyl glutaryl coenzyme A (HMG-CoA) reductase inhibitor and a potential anticholesterol drug candidate |
| 1.4.1.2 | glutamate dehydrogenase |
synthesis |
produktion of L-ornithine in Corynebacterium glutamicum SNK118, by deletion of genes argF, argR, and ncgl2228 to block the degradation of L-ornithine, and overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenases gene from Clostridium saccharobutylicum and glutamate dehydrogenase RocG. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose are achieved by the final strain in a 10-l bioreactor |
| 3.2.1.7 | inulinase |
synthesis |
proposed kinetic model for fructose production defined within temperature and substrate concentration ranges of industrial interest such as 40-60°C and 3-60 g/l, respectively. Model is based on a minimum number of parameters. The hypotheses are always specified and assumed only on the basis of convenience and rational consideration. The kinetic model was successfully validated by comparison with a vast set of experimental results |
| 3.4.24.28 | bacillolysin |
synthesis |
protease N covalently immobilized on agarose can be used for the preparation of acetylated ribonucleosides with only one free hydroxyl group in position C-5', as useful building blocks for the synthesis of monophosphate nucleotides or 5'-deoxyribonucleosides such as Capecitabine |
| 3.2.1.65 | levanase |
synthesis |
protection from aging |
| 1.11.1.7 | peroxidase |
synthesis |
protein engineering to obtain an active and stable HRP variant with reduced surface glycosylation during production in Pichia pastoris. Mutant N13D/N57S/N255D/N268D produced in the Pichia pastoris benchmark strain shows considerable catalytic activity and thermal stability and is less glycosylated |
| 1.14.13.225 | F-actin monooxygenase |
synthesis |
protocol for obtaining high levels of recombinant protein for the redox only portion of Mical. Cold adapted chaperonins alone do not work well for expressing the Mical redox domain, while the use and removal of solubility tags destabilizes. Low-temperature expression, chaperonins and no solubility tag lead to enhanced expression |
| 2.7.2.1 | acetate kinase |
synthesis |
protocol for overproduction of enzyme |
| 3.1.1.4 | phospholipase A2 |
synthesis |
protocol for the overexpression ofisoform PLA2III in Escherichia coli in the form of inclusion bodies, and for its purification and refolding using the Gateway system (Invitrogen) for the expression of a large quantity of the mature with an N-terminal His-tag, and Ni-affinity chromatography for purification. The purified recombinant PLA2III fusion protein is then refolded using a step-wise dialysis approach. About 40 mg purified and active protein is obtained from 1 l of cell culture |
| 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) |
| 4.2.3.135 | DELTA6-protoilludene synthase |
synthesis |
protoilludene is a valuable sesquiterpene and serves as a precursor for several medicinal compounds and antimicrobial chemicals. It can be synthesized by heterologous overexpression of protoilludene synthase in Escherichia coli with coexpression of mevalonate or methylerythritol-phosphate pathway enzymes, and farnesyl diphosphate synthase as a cell factory for protoilludene production |
| 3.5.5.1 | nitrilase |
synthesis |
Pseudomonas aeruginosa RZ44 has the potential to be applied in the biotransformation of nitrile compounds |
| 1.14.12.11 | toluene dioxygenase |
synthesis |
Pseudomonas putida KT2442 (pSPM01) harboring TDO genes can effectively biotransform a wide-range of aromatic substrates into their cis-diols |
| 1.1.2.4 | D-lactate dehydrogenase (cytochrome) |
synthesis |
Pseudomonas stutzeri containing D-lactate dehydrogenase can act as a novel biocatalyst for pyruvate production from DL-lactate |
| 1.1.1.215 | gluconate 2-dehydrogenase |
synthesis |
pulse addition of hydrogen peroxide to synthetic media is beneficial to improve the conversion rate of glucose to 2-oxo-gluconate by 1.47fold |
| 4.2.2.10 | pectin lyase |
synthesis |
purification and surface immobilization using various concentrations of chitosan and glutaraldehyde as cross-linking agent. The immobilized fractions are highly stable over a pH and temperature range from 4-9 and 45-85°C, respectively. Chitosan-immobilized enzyme fractions retain more than 75% of their operational activities even after seven consecutive cycles |
| 3.1.6.1 | arylsulfatase (type I) |
synthesis |
purification method for removing phytoestrogens and related compounds without affecting the enzyme activity. Use of solid phase extraction on a polymeric resin for purification |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
purification of enzyme as crosslinked enzyme aggregates and application for synthesis of enantiopure cyanohydrins |
| 3.5.1.11 | penicillin amidase |
synthesis |
purification of His-tagged enzyme secreted into periplasmic space by immobilized metal-ion affnity chromatography. Maximum specific activity of enzyme is 38.5 U/mg, yield is 70% |
| 1.4.3.2 | L-amino-acid oxidase |
synthesis |
purified aldehyde-tagged 6His-hcLAAO4 is covalently bound to a hexylamine resin via the Calpha-formylglycine residue. The immobilized enzyme can be reused repeatedly to generate phenylpyruvate from L-phenylalanine with a total turnover number of 17600 and is stable for over 40 days at 25 °C |
| 2.7.7.2 | FAD synthase |
synthesis |
purified recombinant FADSCf can be used for the biosynthesis of FAD. Under optimized conditions (0.5 mM FMN, 5 mM ATP and 10 mM Mg2+), the production of FAD reaches 80 mM per mg of enzyme after a 21-hour reaction |
| 4.1.1.7 | benzoylformate decarboxylase |
synthesis |
purified recombinant His-tagged enzyme immobilized on magnetic nanoparticles, microspheres, nanospheres and ferrofluids, is used for enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes. The heterogeneous biocatalyst is offering the ease of immobilization along with the separation steps of metal affinity ligand (Cu2+-iminodiacetic acid) coated magnetic nanoparticles. Reusability of immobilized enzyme for carboligation reactions |
| 2.4.1.5 | dextransucrase |
synthesis |
purified Weissella confusa Cab3 dextransucrase (WcCab3-DSR) is used for in vitro synthesis of dextran and glucooligosaccharides |
| 3.2.2.4 | AMP nucleosidase |
synthesis |
purine nucleotide synthesis in procaryotes |
| 2.4.2.7 | adenine phosphoribosyltransferase |
synthesis |
purine nucleotide synthesis using TthAPRT and TthHPRT (EC 2.4.2.8) |
| 2.6.1.82 | putrescine-2-oxoglutarate transaminase |
synthesis |
putrescine transaminase Pp-SpuC application in the transamination of a comprehensive range of ketones/aldehydes for the production of a variety of benzylamine derivatives. Applications of enzyme Pp-SpuC as a biocatalyst with broad substrate tolerance |
| 1.2.1.99 | 4-(gamma-glutamylamino)butanal dehydrogenase |
synthesis |
PuuC is an active enzyme that can be utilized effectively for several purposes, including biological production of 3-hydroxypropionate |
| 3.5.1.11 | penicillin amidase |
synthesis |
PVA is a pharmaceutically important enzyme to produce 6-aminopenicillanic acid |
| 1.10.3.2 | laccase |
synthesis |
Pycnoporus sp. SYBC-L1 is a potential candidate for laccase production |
| 1.1.99.29 | pyranose dehydrogenase (acceptor) |
synthesis |
pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals |
| 2.6.1.B21 | (R)-amine:2-oxo acid transaminase |
synthesis |
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme |
| 2.6.1.42 | branched-chain-amino-acid transaminase |
synthesis |
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme |
| 2.6.1.30 | pyridoxamine-pyruvate transaminase |
synthesis |
pyridoxamine production by bioconversion is generally preferable for environmental and energetic aspects compared to chemical synthesis. Pyridoxamine is produced from pyridoxine, a readily and economically available starting material, by bioconversion using a Rhodococcus expression system |
| 3.5.1.100 | (R)-amidase |
synthesis |
R-amidase is the first enzyme useful for the enzymatic optical resolution of racemic piperazine-2-tert-butylcarboxamide carried out under mild conditions. Enantiomerically pure piperazine-2-carboxylic acid and its tert-butylcarboxamide derivative are important chiral building blocks for some pharmacologically active compounds such as N-methyl-D-aspartate antagonist for glutamate receptor, cardioprotective nucleoside transport blocker, and HIV protease inhibitor |
| 4.1.1.1 | pyruvate decarboxylase |
synthesis |
Ralstonia eutropha H16 produces polyhydroxybutanoate as an intracellular carbon storage material. The excess carbon can be redirected in engineered strains from polyhydroxybutanoate storage to the production of isobutanol and 3-methyl-1-butanol (branched-chain higher alcohols). Strains of Ralstonia eutropha with isobutyraldehyde dehydrogenase activity, in combination with the overexpression of plasmid-borne, native branched-chain amino acid biosynthesis pathway genes and the overexpression of heterologous ketoisovalerate decarboxylase gene, are employed for the biosynthesis of isobutanol and 3-methyl-1-butanol. One mutant strain produces over 180 mg/l branched-chain alcohols in flask culture, and is significantly more tolerant of isobutanol toxicity than wild-type. After the elimination of genes ilvE, bkdAB, and aceE, the production titer improves to 270 mg/l isobutanol and 40 mg/l 3-methyl-1-butanol. Under semicontinuous flask cultivation, the strain grows and produces more than 14 g/l branched-chain alcohols over the duration of 50 days |
| 6.3.1.2 | glutamine synthetase |
synthesis |
rapid and scalable two-step protocol for expression and purification of glutamine synthetase in an auxotrophic Escherichia coli strain utilizing differential precipitation by divalent cations followed by affinity chromatography to produce suitable quantities of homogenous material for structural characterization |
| 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% |
| 5.1.3.31 | D-tagatose 3-epimerase |
synthesis |
rare sugar production |
| 2.1.1.142 | cycloartenol 24-C-methyltransferase |
synthesis |
rational drug target design based on structure-function-relation |
| 2.4.1.144 | beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase |
synthesis |
RC12 cells, apheochromocytoma cell line, transfected with enzyme gene, result in suppression of neurite outgrowth induced by costimulation of epidermal growth factor and integrins. Epidermal growth factor receptor-mediated ERK-activation is blocked in transfectants. Epidermal growth factor receptor of transfectants is modified by bisecting GlcNAc in its N-glycan structures |
| 2.7.7.48 | RNA-directed RNA polymerase |
synthesis |
RdRp from the bacteriophage phi6 can be used to generate dsRNA for RNA interference, RNAi, applications, resulting in in vivo gene silencing. RNA molecules that are radioactively or fluorescently labeled using poly(A) polymerase can be used as probes in a wide variety of applications |
