EC Number   |
Recommended Name |
Application |
|---|
   4.1.1.52 | 6-methylsalicylate decarboxylase |
biotechnology |
biotechnological de novo production of m-cresol from sugar in complex yeast extract-peptone medium with the yeast Saccharomyces cerevisiae. A heterologous pathway based on the decarboxylation of the polyketide 6-methylsalicylic acid is introduced into a CEN.PK yeast strain. Overexpression of codon-optimized 6-methylsalicylic acid synthase from Penicillium patulum together with activating phosphopantetheinyl transferase npgA from Aspergillus nidulans results in up to 367 mg/l 6-methylsalicylic acid production. Additional genomic integration of the genes have a strongly promoting effect and 6-methylsalicylic acid titers reach more than 2 g/l. Simultaneous expression of 6-methylsalicylic acid decarboxylase patG from Aspergillus clavatus leads to the complete conversion of 6-methylsalicylic acid and production of up to 589 mg/L m-cresol |
 4.1.1.61 | 4-hydroxybenzoate decarboxylase |
biotechnology |
use of enzyme for conversion of phenol into 4-hydroxybenzoic acid |
| 4.1.1.76 | arylmalonate decarboxylase |
biotechnology |
enzyme is of biotechnological interest for its use in the synthesis of fine chemicals |
| 4.1.1.123 | phenyl-phosphate phosphatase/carboxylase |
biotechnology |
the enzyme system may be useful for biotechnical phenol carboxylation |
| 4.1.2.4 | deoxyribose-phosphate aldolase |
biotechnology |
DERA has the potential to resist high concentrations of acetaldehyde and may serve as an industrial catalyst |
| 4.1.2.4 | deoxyribose-phosphate aldolase |
biotechnology |
efficient process for the production of thermophilic DERA designed from the point of view of recombinant enzyme concentration and productivity, which is economically and technically viable and can be used as a guide for production of other synthetically useful enzymes |
| 4.1.2.5 | L-threonine aldolase |
biotechnology |
development of a growth-dependent selection system for identification of L-threonine aldolases in Pseudomonas putida KT2440. The functionality is demonstrated with different growth studies by introducing recombinant, nonnative The functionality was demonstrated with different growth studies by introducing recombinant, nonnative threonine aldolases into the selection strain, restoring its deficiency in growth in minimal medium supplemented with DL-threo-beta-phenylserine as sole carbon source |
| 4.1.2.9 | phosphoketolase |
biotechnology |
expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds |
| 4.1.2.9 | phosphoketolase |
biotechnology |
pathway engineering advances in a high-potential alternative route, the phosphoketolase pathway, which facilitates bypass of pyruvate decarboxylation and enables complete carbon conservation in bioprocesses targeting pentose phosphate pathway and/or acetyl-CoA-derived products |
| 4.1.2.22 | fructose-6-phosphate phosphoketolase |
biotechnology |
expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds |
| 4.1.2.48 | low-specificity L-threonine aldolase |
biotechnology |
a continuous bioconversion system for L-threo-3,4-dihydroxyphenylserine production is developed that uses whole-cell biocatalyst of recombinant Escherichia coli expressing L-TA genes cloned from Streptomyces avelmitilis MA-4680. Maximum conversion rates are observed at 2 M glycine, 145 mM 3,4-dihydroxybenzaldehyde, 0.75% Triton-X, 5 g Escherichia coli cells/l, pH 6.5 and 10°C. In the optimized condition, overall productivity is 8 g/l |
| 4.1.3.3 | N-acetylneuraminate lyase |
biotechnology |
coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase |
| 4.1.3.3 | N-acetylneuraminate lyase |
biotechnology |
efficient method for N-acetyl-D-neuraminic acid production using coupled bacterial cells with a safe temperature-induced system, a precursor for producing many pharmaceutical drugs such as zanamivir which have been used in clinical trials to treat and prevent the infection with influenza virus, such as the avian influenza virus H5N1 and the current 2009 H1N1 |
| 4.1.3.3 | N-acetylneuraminate lyase |
biotechnology |
chemoenzymatic synthesis of N-acetyl-D-neuraminic acid from N-acetyl-D-glucosamine and pyruvate |
| 4.1.3.3 | N-acetylneuraminate lyase |
biotechnology |
cross-linked enzyme aggregates |
| 4.1.3.27 | anthranilate synthase |
biotechnology |
development of a microbial system for the environmentally-compatible synthesis of anthranilate generated by metabolic engineering of trpD gene from strain W3110 trpD9923 |
| 4.1.3.27 | anthranilate synthase |
biotechnology |
development of ASA2 as a chloroplast selective marker, which is important not only for biosafety reasons, but also for practical reason due to the scarcity of primary selective markers available |
| 4.1.3.27 | anthranilate synthase |
biotechnology |
Oryza sativacalli overexpressing OASA1D:OASA1D is a system for the production of significant amounts of pharmacologically useful indole alkaloids in rice |
| 4.1.99.1 | tryptophanase |
biotechnology |
encapsulation of enzyme in wet nanoporous silica gels to selectively stabilize tertiary and quarternary protein conformations and to develop bioreactors and biosensors |
| 4.1.99.2 | tyrosine phenol-lyase |
biotechnology |
encapsulation of enzyme in wet nanoporous silica gels to selectively stabilize tertiary and quarternary protein conformations and to develop bioreactors and biosensors |
| 4.1.99.2 | tyrosine phenol-lyase |
biotechnology |
tyrosine phenol lyase modifies and synthesizes natural and non-natural amino acids, synthesizes precursor of a large number of relevant compounds and plays an important role in phenolic waste treatment |
| 4.1.99.3 | deoxyribodipyrimidine photo-lyase |
biotechnology |
a new class of photolyases with specificity for cyclobutane pyrimidine dimers in ssDNA is defined. Members of these branch are found in bacteria, plants, and animals, and are designated Cry-DASH, because of the lack of significant photorepair activity on dsDNA |
| 4.1.99.3 | deoxyribodipyrimidine photo-lyase |
biotechnology |
it should be possible to perform wavelength tuning of the Thermus photolyase by using artificial flavin chromophores and photolyase variants whose antenna chromophore-binding sites are reengineered by molecular modeling and mutagenesis |
| 4.2.1.3 | aconitate hydratase |
biotechnology |
molecular chaperones GroEL/GroES are co-expressed with soluble, biologically active recombinant aconitase in Escherichia coli by cultivation in a bioreactor at different temperatures under optimized conditions. The yield of functional aconitase is enhanced, either in presence of co-expressed GroEL/ES or at low temperature cultivation. The outcome from the chaperone assisted folding of aconitase is more pronounced at lower temperature |
| 4.2.1.20 | tryptophan synthase |
biotechnology |
enzyme is a target for structure-based design of herbicides |
| 4.2.1.30 | glycerol dehydratase |
biotechnology |
development of an economical and eco-friendly biological process for the production of 1,3-propanediol by an operon harboring the dhaB1, dhaB2, and yqhD genes, from renewable resources |
| 4.2.1.47 | GDP-mannose 4,6-dehydratase |
biotechnology |
repression of the GMD gene is thus very useful for deleting immunogenic total fucose residues and facilitating the production of pharmaceutical glycoproteins in plants |
| 4.2.1.66 | cyanide hydratase |
biotechnology |
searching for enzymes in the bioremediation of cyanide-containing waste |
| 4.2.1.81 | D(-)-tartrate dehydratase |
biotechnology |
constitutive production of enzyme for selective cleavage of racemic tartaric acid and quantitative detection of D(-)-tartrate |
| 4.2.1.104 | cyanase |
biotechnology |
analysis of strain characteristics for biotechnological application, detoxification of cyanide- or thiocyanate-containing soils and industrial effluents |
| 4.2.1.108 | ectoine synthase |
biotechnology |
inducible recombinant enzyme expression in Escherichia coli confers the capability to grow on high concentration of osmolytes by increasing the osmotolerance via L-ectoine production |
| 4.2.1.108 | ectoine synthase |
biotechnology |
ectoine has importance in dermopharmacy as anti ageing agents in skin creams, as components of shampoo, for oral care and as adjuvants for vaccines |
| 4.2.1.119 | enoyl-CoA hydratase 2 |
biotechnology |
recombinant 46 kDa hydratase 2 survives in a purified form under storage, thus being the first protein of this type amenable to application as a tool in metabolic studies |
| 4.2.1.127 | linalool dehydratase |
biotechnology |
possible biotechnological applications of Ldi, in particular, are industrial butadiene and isoprene production from renewable sources |
| 4.2.1.134 | very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase |
biotechnology |
the enzyme is a potential target for biotechnological optimization of the production of docosahexenoic acid (DHA) in the Aurantiochytrium sp. thraustochytrid strain PKUSW7 |
| 4.2.1.135 | UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) |
biotechnology |
assay targets enzymes involved in the biosynthesis of the unusual bacterial sugar diNAcBac and the transfer of diNAcBac-phosphate to UndP. This multienzyme assay, together with the established assays for the individual enzymes, can be used to screen for inhibitors, and may be used to evaluate substrate flux along the inhibited pathway. This assay is optimized for maximum sensitivity to inhibition of PglF, PglE, PglD, and PglC by balancing the enzyme concentrations such that each is partially rate determining |
| 4.2.2.2 | pectate lyase |
biotechnology |
optimization of fermentation conditions |
| 4.2.2.2 | pectate lyase |
biotechnology |
the enzyme can be used for bioscouring of cotton |
| 4.2.2.2 | pectate lyase |
biotechnology |
the pectinase preparation from Bacillus macerans can compete with the commercial preparations for the process of cotton fabric boil off |
| 4.2.2.2 | pectate lyase |
biotechnology |
a combined (enzymatic and chemical) process using a Bacillus pumilus strain (DKS1), isolated from the soil, is used to degum ramie bast fibres. Results indicate the process provides an economical and eco-friendly method for the small scale as well as large-scale degumming of decorticated ramie fibre. Results are of importance for the textile as well as paper industry |
| 4.2.2.2 | pectate lyase |
biotechnology |
application of a commercial pectinase for a range of concentrations and treatment times creates pectin-free textiles with low wax content. Assessment of physicochemical properties such as, wettability, whiteness index, polymerization degree, crystallinity index, color depth, as well as low-stress mechanical properties, proves that bioscouring can be as much efficient as the conventional alkaline treatment |
| 4.2.2.2 | pectate lyase |
biotechnology |
enhancing PGL production by controlling the optimal ratio provides an alternative approach to enhance heterologous protein production with Pichia pastoris |
| 4.2.2.2 | pectate lyase |
biotechnology |
parameters for maximum production of PGL by yeast strain Debaryomyces nepalensis in bioreactor are determined: optimal levels of pH, aeration and agitation rate is found to be 7.0, 300 rpm and 1 vvm, respectively. Combined feeding of inducer (lemon peel) and carbon source (galactose) at 12 h is the best strategy for enhanced production of PGL. The production is increased by 1.8fold and productivity 1.4fold for PGL when compared to batch culture |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biotechnology |
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biotechnology |
most of Pseudomonas strains have copious alginates enclosing the bacteria cells, which makes it difficult to transfer exogenous DNA into the cells during transformation. Pretreatment of Pseudomonas sp. QDA with alginate lyase before electroporation increases transformation efficiency approximately 10000fold than without pretreatment of alginate lyase, and a high transformation efficiency nearly the same as that of alginate production deficient mutant is obtained. Among the alginate lyases tested, AL2 is the most effective enzyme for pretreatment. This electroporation procedure is also efficient for Pseudomonas aeruginosa FRD1 (mucoid) and PAO1 (non-mucoid) |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biotechnology |
a new highly specific and sensitive capillary electrophoresis method for the determination of the total alginic acid (AA) content in pharmaceutical formulations is described by means of capillary electrophoresis at 230 nm after treatment with alginate lyase and separation of unsaturated products, DELTA-oligomers (DELTA-HexA-[HexA]n), in particular, DP3 (DELTA-HexA-HexA-HexA) and DP4 (DELTAHexA-HexA-HexA-HexA). The capillary electrophoresis method is applied to the determination of AA content of both solid and liquid formulations that also contain antacid ingredients, mainly aluminium, sodium and potassium bicarbonate, and emulsifying and flavouring agents |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biotechnology |
the algino-oligosaccharides show an elicitor activity stimulating the accumulation of phytoalexin and inducing phenylalanine ammonia lyase in soybean cotyledon, and antimicrobial activity on Pseudomonas aeruginosa |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biotechnology |
the bacterium A7 is shown to be alginate lyase-producing in genus Gracilibacillus and effective in degrading alginate to oligosaccharides in wakame during composting process |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biotechnology |
controlled mono-PEGylation of A1-III alginate lyase mutant A53C produces a conjugate with wild type levels of activity. The PEGylated mutant exhibits enhanced solution phase kinetics with bacterial alginate. In vitro binding studies with both enzyme-specific antibodies, from immunized New Zealand white rabbits, and a single chain antibody library, derived from a human volunteer show that the PEGylated enzyme is substantially less immunoreactive. More than 90% of adherent, mucoid, Pseudomonas aeruginosa biofilms are removed from abiotic surfaces following a one h treatment with the PEGylated mutant, whereas the wild type enzyme removes only 75% of biofilms in parallel studies |
| 4.2.2.14 | glucuronan lyase |
biotechnology |
a glucuronan lyase is immobilized on a monolithic Convective Interaction Media disk. Degradations of three glucuronans with various O-acetylation degrees is investigated and compared with degradations using free enzyme. The immobilized glucuronan lyase is inhibited by the O-acetylation degree like the free enzyme. 1H NMR analyses are used to study the O-acetylation degree of oligoglucuronans and demonstrate that the average degrees of polymerization are inclusive between 4 and 13 after 24 h of degradation. This first immobilization of a glucuronan lyase constitutes a tool to produce oligoglucuronans |
| 4.2.2.16 | levan fructotransferase (DFA-IV-forming) |
biotechnology |
production of Arthrobacter levan fructotransferase from recombinant Escherichia coli at high levels via secretion directed by a novel N-terminal motif, TMITNSSSVP. A large amount of extracellular recombinant levan fructotransferase can be produced with high productivity through cost-effective processes |
| 4.2.2.18 | inulin fructotransferase (DFA-III-forming) |
biotechnology |
improved enzyme for large scale production of low-calorie sweet food additive |
| 4.2.2.18 | inulin fructotransferase (DFA-III-forming) |
biotechnology |
large scale production of sweet food additive DFA III via recombinant expression in E. coli, genetic engineering of the enzyme for enlarged thermotolerance, immobilization of the enzyme on alginate beads |
| 4.2.2.20 | chondroitin-sulfate-ABC endolyase |
biotechnology |
bond strength of two etch-and-rinse adhesives to chondroitinase ABC treated dentin is investigated. Human extracted molars are treated with chondroitinase ABC. Increased mean values of microtensile bond strength and reduced nanoleakage expression are shown for both adhesives after chondroitinase ABC treatment of the dentin surface. This study supports the hypothesis that adhesion can be enhanced by removal of chondroitin 4/6 sulfate and dermatan sulfate, probably due to a reduced amount of water content and enlarged interfibrillar spaces |
| 4.2.2.21 | chondroitin-sulfate-ABC exolyase |
biotechnology |
preservation of ChABC activity during release by immobilizing ChABC in chitosan nerve conduits and encapsulating ChABC in poly(DL-lactic acid) microspheres using an appropriate stabilizer. Immobilizing ChABC in nerve conduitss markedly improves its stability. The activity of ChABC that is immobilized in chitosan nerve conduits by ionic bonding is 0.07 U/mg. 48% of this activity is retained at 48 h after immobilization. Poly(DL-lactic acid) microspheres, fabricated by the double emulsion method, are applied as carriers in the controlled release of ChABC. Stabilizers, including nanogold of 10 nm, polylysine of Mw 500-2000 and polylysine of Mw 20000-30000, are added to microspheres to maintain the activity of ChABC. Polylysine stabilizes ChABC most effectively. The ChABC activity is 0.0162 U/ml after seven days of release |
| 4.2.3.6 | trichodiene synthase |
biotechnology |
mutants D98E, D99E, D102E generate varying proportions of anomalous sesquiterpenes |
| 4.2.3.25 | S-linalool synthase |
biotechnology |
the enzyme can be used to modify the flavor/nuritional value of vegetables, e.g. tomato fruits, by enzyme expression in transgenic plants |
| 4.2.3.25 | S-linalool synthase |
biotechnology |
biotechnological potential of the engineered wine yeast to modify the sensorial qualities of wine |
| 4.2.99.18 | DNA-(apurinic or apyrimidinic site) lyase |
biotechnology |
is frequently used in gene technology due to its strong exonucleolytic activity |
| 4.2.99.21 | isochorismate lyase |
biotechnology |
alternative computational rational approach to improve the secondary catalytic activity of enzymes, taking as a test case the IPL enzyme. The approach is based on the use of molecular dynamic simulations employing hybrid quantum mechanics/molecular mechanics methods that allow describing breaking and forming bonds |
| 4.3.1.1 | aspartate ammonia-lyase |
biotechnology |
overview on commercial applications |
| 4.3.1.1 | aspartate ammonia-lyase |
biotechnology |
enhancement of recombinant protein production in Escherichia coli by coproduction of aspartase. The excretion of acetate by the aerobic growth of Escherichia coli on glucose is a manifestation of imbalanced flux between glycolysis and the tricarboxylic acid (TCA) cycle. This may restrict the production of recombinant proteins in E. coli, due to the limited amounts of precursor metabolites produced in TCA cycle. To approach this issue, an extra supply of intermediate metabolites in TCA cycle is made by conversion of aspartate to fumarate, a reaction mediated by the activity of L-aspartate ammonia-lyase |
| 4.3.1.1 | aspartate ammonia-lyase |
biotechnology |
putative and attractive enzyme for the enantioselective synthesis of N-substituted aspartic acids |
| 4.3.1.1 | aspartate ammonia-lyase |
biotechnology |
a complete biocatalytic process to synthesize high concentrations of L-aspartate catalyzed by aspartase from Bacillus sp. YM55-1 (AspB) is established using an immobilized enzyme in three different supports. MANA-agarose derivative could be selected as the most suitable biocatalyst for the synthesis of Asp due to the simplicity of the method and performance |
| 4.3.1.2 | methylaspartate ammonia-lyase |
biotechnology |
Fusobacterium varium can simultaneously utilize both glucose and L-glutamate as energy sources, intracellular concentrations of methylaspartate ammonia-lyase is elevated when the bacterium is cultured in media supplemented with excess L-glutamate |
| 4.3.1.12 | ornithine cyclodeaminase |
biotechnology |
expression of ocd from Pseudomonas putida in an ornithine overproducing platform strain with deletions of argR and argF (ORN1) from Corynebacterium glutamicum results in proline production with yields up to 0.31 g proline/g glucose |
| 4.3.1.14 | 3-Aminobutyryl-CoA ammonia-lyase |
biotechnology |
lysine fermentation pathway |
| 4.3.1.24 | phenylalanine ammonia-lyase |
biotechnology |
compared to the free enzyme, the PAL-CLEA exhibit increased stability of the enzyme against various deactivating conditions such as pH, temperature, denaturants, and organic solvents and show higher storage stability than its soluble counterpart. Additionally, PAL-CLEAs can be recycled at least for 12 consecutive batch reactions without dramatic activity loss, increases the commercial potential of PAL for synthesis of L-phenylalanine |
| 4.3.1.24 | phenylalanine ammonia-lyase |
biotechnology |
the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria |
| 4.3.3.2 | strictosidine synthase |
biotechnology |
modulating the substrate specificity of strictosidine synthase is a critical step toward indole alkaloid pathway engineering to yield nonnatural alkaloids |
| 4.3.3.2 | strictosidine synthase |
biotechnology |
redesigning the substrate specificity of strictosidine synthase is an important step toward re-engineering the TIA pathway to produce products with novel or improved biological properties |
| 4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
biotechnology |
enzyme is a target for herbicide and anti-microbial action |
| 4.4.1.1 | cystathionine gamma-lyase |
biotechnology |
use of strain as adjunct starter in cheese making |
| 4.4.1.4 | alliin lyase |
biotechnology |
lachrymatory factor synthase and alliinase function in tandem, with the alliinase furnishing the sulfenic acid substrate on which the lachrymatory factor synthase acts. The lachrymatory factor synthase modulates the formation of biologically active thiosulfinates that are downstream of the alliinase in a manner dependent upon the relative concentrations of the lachrymatory factor synthase and the alliinase. These observations suggest that manipulation of lachrymatory factor synthase-to-alliinase ratios in plants displaying this system may provide a means by which to rationally modify organosulfur small molecule profiles to obtain desired flavor and/or odor signatures, or increase the presence of desirable biologically active small molecules |
| 4.5.1.1 | DDT-dehydrochlorinase |
biotechnology |
positive correlation of enzyme activity and resistance against DDT |
| 4.5.1.1 | DDT-dehydrochlorinase |
biotechnology |
positive correlation of enzyme activity and resistance against DDT, and also between enzyme activity and GST activity |
| 4.5.1.1 | DDT-dehydrochlorinase |
biotechnology |
positive correlation of enzyme activity and resistance against DDT, non-correlation between enzyme activity and GST activity |
| 4.6.1.18 | pancreatic ribonuclease |
biotechnology |
synthesis of molecularly imprinted polymers from the monomers styren and polyethyleneglycol 400 dimethacylate with high rebinding efficiency of RNase A to polymer. Polymers show high selectivity for RNase A and high stability |
| 4.6.1.19 | ribonuclease T2 |
biotechnology |
isolate could be a novel renewable source of DNase-free RNase enzyme |
| 4.6.1.22 | Bacillus subtilis ribonuclease |
biotechnology |
bacisubin is an antifungal protein |
| 4.6.1.24 | ribonuclease T1 |
biotechnology |
the RNase G mutation could be applied in the breeding of producer strains of pyruvate and its derivatives such as valine |
| 4.8.1.2 | aliphatic aldoxime dehydratase |
biotechnology |
nitrile compounds are important intermediates in some industrial processes to produce nylon and acrylic fibers, insecticides, and pharmaceuticals. A more environmentally benign process of aldoxime dehydration is needed, for which a biological dehydration of aldoxime is a possible candidate |
| 4.98.1.1 | protoporphyrin ferrochelatase |
biotechnology |
co-expression with ferrochelatase along with the addition of a small amount of delta-aminolevulinic acid, is sufficient to produce fully incorporated heme protein. This method is applicable for both Cys-ligated and His-ligated heme proteins |
| 4.99.1.2 | alkylmercury lyase |
biotechnology |
coexpression of enzyme and mercuric reductase in Arabidopsis thaliana leads to growth on 50fold higher methylmercury concentrations than wild-type plants |
| 4.99.1.2 | alkylmercury lyase |
biotechnology |
engineering of enzyme as to be targeted for accumulation in the endoplasmic reticulum and for secretion to the cell wall rendering the expressing plants resistant to organic mercury |
| 5.1.1.1 | alanine racemase |
biotechnology |
use of enzyme gene as a promoter-screening tool for identification of conditional promoters in Lactobacillus plantarum. Screen for clones capable of complementing the D-alanine auxotroph phenotype of enzyme deletion mutant in media containing enzyme inhibitor D-cycloserine |
| 5.1.1.5 | lysine racemase |
biotechnology |
enzyme is a novel non-antibiotic selectable marker for plant transformation |
| 5.1.1.10 | amino-acid racemase |
biotechnology |
since commercially available D-Trp is chemically synthesized and expensive a mutant BAR protein might represent an effective method to synthesize D-Trp |
| 5.1.1.10 | amino-acid racemase |
biotechnology |
an enzyme lyophilisate of amino acid racemase from Pseudomonas putida is used for in situ racemization. Crystallization experiments accompanied by enzymatic racemization lead to a significant increase of crystallized L-Asn |
| 5.1.1.17 | isopenicillin-N epimerase |
biotechnology |
The results indicate that Penecillium chrysogenum can be used as heterologous host for the production of deacetylcephalosporin C |
| 5.1.1.17 | isopenicillin-N epimerase |
biotechnology |
production of beta-lactam antibiotics |
| 5.1.2.2 | mandelate racemase |
biotechnology |
the demonstrated application of a membrane bioreactor will be a useful method for large-scale dynamic kinetic resulution (DKR) of mandelic acid and for possible other bioconversions in organic media |
| 5.1.3.1 | ribulose-phosphate 3-epimerase |
biotechnology |
efficient utilization of the available glucose and xylose in the lignocellulosic hydrolysates is the important issue for economic cellulosic ethanol production. Simultaneous utilization of xylose is realized by the coupling of glucose metabolism and xylose utilization through RPE1 deletion in xylose-utilizing Saccharomyces cerevisiae |
| 5.1.3.8 | N-acylglucosamine 2-epimerase |
biotechnology |
coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase |
| 5.1.3.8 | N-acylglucosamine 2-epimerase |
biotechnology |
efficient method for N-acetyl-D-neuraminic acid production using coupled bacterial cells with a safe temperature-induced system, a precursor for producing many pharmaceutical drugs such as zanamivir which have been used in clinical trials to treat and prevent the infection with influenza virus, such as the avian influenza virus H5N1 and the current 2009 H1N1 |
| 5.1.3.14 | UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) |
biotechnology |
production of erythropoietin (EPO) in Chinese Hamster Ovary (CHO) cells |
| 5.2.1.5 | linoleate isomerase |
biotechnology |
the enzyme can be useful for biocatalysis of linoleic acid to conjugated linoleic acid |
| 5.3.1.5 | xylose isomerase |
biotechnology |
putative use of lignocellulosic biomass as feedstock for the chemical industry |
| 5.3.1.8 | mannose-6-phosphate isomerase |
biotechnology |
effective use of enzyme gene as selectable marker gene for transformation of embryogenic calli of Carica papaya |
| 5.3.1.8 | mannose-6-phosphate isomerase |
biotechnology |
selection system for transformation of onion using enzyme gene and Agrobacterium. Transformation rates are around 25% |
