EC Number   |
Recommended Name  |
Application |
|---|
  1.1.1.275 | (+)-trans-carveol dehydrogenase |
biotechnology |
applicability of strains with high enzyme content or recombinant overproducing strains for production of (+)-carvone, which is used as a flavor compound |
  1.1.1.227 | (-)-borneol dehydrogenase |
biotechnology |
the gene encoding the borneol dhdrogenase is a target for metabolic engineering for improvement of essential oil production |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
biotechnology |
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
biotechnology |
glucuronoyl esterases are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid in plant cell walls. This activity renders glucuronoyl esterases attractive research targets for biotechnological applications. One of the factors impeding the progress in glucuronoyl esterases research is the lack of suitable substrates. A facile preparation is described of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl beta-D-glucuronides for qualitative and quantitative glucuronoyl esterase assay coupled with beta-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of glucuronoyl esterase in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries |
| 2.7.4.25 | (d)CMP kinase |
biotechnology |
CMP kinase and actetate kinase in a whole cell-biocatalysis to obtain CTP |
| 2.3.3.21 | (R)-citramalate synthase |
biotechnology |
fermentation of C5 and C6 sugars to ethanols and other metabolites under thermophilic conditions |
| 2.1.1.140 | (S)-coclaurine-N-methyltransferase |
biotechnology |
CNMT should be quite useful for biotransformation of the intermediates of alkaloid biosynthesis to N-methyltransferred products |
| 3.2.1.63 | 1,2-alpha-L-fucosidase |
biotechnology |
the purified alpha1,2-fucosidase and L-fucose dehydrogenase have sufficiently high activities in phosphate-buffered saline (pH 7.0) at 37 °C, making it possible to develop a one-pot method for the quantitative determination of 2'-fucosyllactose in fermentation samples. The application of this method is more convenient for quantifying 2'-fucosyllactose in a variety of samples that may be obtained from different phases of the biotechnological production of this oligosaccharide. The method is useful for simple and rapid screening of active variants during the development of any industrially important microbial strain producing 2'-fucosyllactose |
| 2.4.1.211 | 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase |
biotechnology |
LNBP is cultured with sucrose phosphorylase, UDP-glucose hexose 1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase to produce beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine using sucrose as substrate in a 10l reaction mixture, 500 mmol beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine are produced after 600 h, beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine can be used as bifidus factor in human milk |
| 2.4.1.18 | 1,4-alpha-glucan branching enzyme |
biotechnology |
RNAi technology is applied to suppress the expression of starch branching enzyme IIa and IIb and to increase amylose content in maize endosperm, and stably inherit high-amylose maize lines |
| 2.4.1.18 | 1,4-alpha-glucan branching enzyme |
biotechnology |
RNAi technology is applied to suppress the expression of starch branching enzyme IIa and IIb and to increase amylose content in maize endosperm, and stably inherit high-amylose maize lines. Transgenic maize lines with amylose content of up to 55.89% are produced, which avoid the significant decreases in starch content and grain yield that occur in high-amylose starch branching enzyme IIb gene mutant |
| 2.4.2.24 | 1,4-beta-D-xylan synthase |
biotechnology |
enzyme activity is hardly affected by addition of organic solvents |
| 1.1.1.267 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase |
biotechnology |
DXR plays a role in the methyl-D-erythritol 4-phosphate pathway, which is responsible for the biosynthesis of a substantial number of natural compounds of biological and biotechnological importance and is considered as a target to develop new herbicides and antimicrobial drugs |
| 2.2.1.7 | 1-deoxy-D-xylulose-5-phosphate synthase |
biotechnology |
increase production level of CoQ10 by coexpression of decaprenyl diphosphate synthase and 1-deoxy-D-xylulose 5-phosphate synthase isolated from Rhizobium radiobacter ATCC 4718 in recombinant Escherichia coli is shown |
| 2.3.1.167 | 10-deacetylbaccatin III 10-O-acetyltransferase |
biotechnology |
optimizing the semi-biosynthetic method in bacteria potentially provides a practical means of developing commercial-scale production of baccatin III analogs, which serve as key intermediates in the semi-synthesis of second-generation taxols |
| 2.5.1.32 | 15-cis-phytoene synthase |
biotechnology |
creation of marker-free transgenic plants |
| 2.5.1.32 | 15-cis-phytoene synthase |
biotechnology |
developement nutritional plants enriched with carotenoids |
| 1.1.1.274 | 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming) |
biotechnology |
enzyme is a target for the construction of a NADH-utilizing mutant strain in the industrial production of vitamin C |
| 1.13.11.9 | 2,5-dihydroxypyridine 5,6-dioxygenase |
biotechnology |
the enzyme catalyzes one step in a new process of detoxification/biotransformation of N-heterocyclic aromatic compounds |
| 2.6.1.86 | 2-amino-4-deoxychorismate synthase |
biotechnology |
conversion of aminodeoxychorismate synthase into anthranilate synthase employing a bioinformatics method for predicting mutations required to functionally interconvert homologous enzymes. Complementation of an anthranilate synthase-deficient strain of Escherichia coli grown on minimal medium leads to several aminodeoxychorismate synthase mutants that allow growth in 6 days compared to 2 days for wild-type anthranilate synthase. The purified mutant enzymes catalyze the conversion of chorismate to anthranilate at rates that are about 50% of the rate of wild-type aminodeoxychorismate synthase-catalyzed conversion of chorismate to aminodeoxychorismate. The residues mutated do not contact the substrate |
| 2.7.7.60 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
biotechnology |
high-throughput methods for the screening of 2C-methyl-D-erythritol synthase IspC protein, 4-diphosphocytidyl-2C-methyl-D-erythritol synthase IspD protein, 4-diphosphocytidyl-2Cmethyl-D-erythritol kinase IspE protein, and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase IspF protein, against large compound libraries. Assays use up to three auxiliary enzymes monitored at 340 and all robust |
| 1.3.1.31 | 2-enoate reductase |
biotechnology |
enoate reductase(ER)-functionalized poplar powder(FPP) and glucose-6-phosphate dehydrogenase(GDH)-FPP enable the continuous conversion of 4-(4-methoxyphenyl)-3-buten-2-one with NAD+ recycling. The immobilization strategy is simple and inexpensive and exploits a method for the immobilization and application of enoate reductase and its cofactor recycling system |
| 1.1.1.312 | 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase |
biotechnology |
production of 2-pyrone-4,6-dicarboxylic acid from protocatechuate as a precursor for biopolymers |
| 1.1.1.312 | 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase |
biotechnology |
engineering plants with the proposed de-novo PDC pathway provides an avenue to enrich biomass with a value-added co-product while simultaneously improving biomass quality for the supply of fermentable sugars. Implementing this strategy into bioenergy crops has the potential to support existing microbial fermentation approaches that exploit lignocellulosic biomass feedstocks for PDC production |
| 1.1.99.30 | 2-oxo-acid reductase |
biotechnology |
preparative scale production of pyruvate from (R)-lactate in an enzyme-membrane reactor with coupled electrochemical regeneration of the artificial mediator anthraquinone-2,6-disulfonate, process modeling and calculation |
| 1.13.12.19 | 2-oxoglutarate dioxygenase (ethene-forming) |
biotechnology |
different cultivation factors on ethylene formation in Saccharomyces cerevisiae expressing the EFE in continuous cultures is investigated. Main finding is that oxygen availability is crucial for ethylene production. By employing three different nitrogen sources it is shown that the nitrogen source available can both improve and impair the ethylene productivity |
| 1.13.12.19 | 2-oxoglutarate dioxygenase (ethene-forming) |
biotechnology |
EFE is a promising biotechnology target because the expression of a single gene is sufficient for ethylene production in the absence of toxic intermediates |
| 1.1.1.149 | 20alpha-hydroxysteroid dehydrogenase |
biotechnology |
a process is developed that that allows the production of 20alpha- dihydrodydrogesterone at technical scale (several grams of 20a-DHD per week and fermenter). Genetic improvement of the production strain, an increase of substrate solubility by addition of ß-cyclodextrin, and the development of a sophisticated high-cell density fermentation at pilot scale are employed. By usage of the exemplary substrate progesterone, it is hsown that this innovative fission yeast-based whole cell biotransformation process is transferable to the conversion of other AKR1C1 substrates without special adaptation |
| 1.1.1.149 | 20alpha-hydroxysteroid dehydrogenase |
biotechnology |
an aldo-keto reductases-dependent whole-cell biotransformation process is established that can be used for production of human aldo-keto reductases metabolites on a large scale |
| 2.1.1.143 | 24-methylenesterol C-methyltransferase |
biotechnology |
SMT2-1 overexpression leads to changes of phytosterol content and the ratio of campesterol to sitosterol in fiber cell. At the rapid elongation stage of fiber cell, total phytosterol and sitosterol contents are increased while campesterol content is decreased in transgenic fibers. The ratio of campesterol to sitosterol declines strikingly. The transgenic fibers are shorter and thicker than control fibers. Exogenous application of sitosterol or campesterol inhibits control fiber cell elongation in cotton ovule culture system in vitro. Campesterol treatment partially rescues fiber elongation in overexpressing plants |
| 3.1.3.7 | 3'(2'),5'-bisphosphate nucleotidase |
biotechnology |
GhHL1 is a functional and good candidate gene that might be used to improve salt tolerance in plants |
| 4.3.1.14 | 3-Aminobutyryl-CoA ammonia-lyase |
biotechnology |
lysine fermentation pathway |
| 2.5.1.54 | 3-deoxy-7-phosphoheptulonate synthase |
biotechnology |
increased production of aromatic amino acids in E. coli mutants with modified phosphoenolpyruvate metabolism and enhanced transketolase activity |
| 2.5.1.54 | 3-deoxy-7-phosphoheptulonate synthase |
biotechnology |
E. coli strains, overproducing the enzyme, excrete it to the medium, which can also be used as a bioindicator for enhanced carbon commitment into the pathway |
| 2.5.1.54 | 3-deoxy-7-phosphoheptulonate synthase |
biotechnology |
fruit-specific manipulation of the conversion of primary to specialized metabolism, e.g. by expressing 3-deoxy-7-phosphoheptulonate synthase in tomato fruits, is an attractive approach for improving fruit aroma and flavour qualities as well as discovering novel fruit-specialized metabolites. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview |
| 2.5.1.19 | 3-phosphoshikimate 1-carboxyvinyltransferase |
biotechnology |
conferring glyphosate tolerance in transgenic crop plants |
| 2.5.1.19 | 3-phosphoshikimate 1-carboxyvinyltransferase |
biotechnology |
glyphosate tolerance in bacteria |
| 2.5.1.19 | 3-phosphoshikimate 1-carboxyvinyltransferase |
biotechnology |
strain PCC6803 DnaE intein N-terminal and C-terminal splicing domains can reconstitute EPSPS activities and glyphosate resistance in plant |
| 3.1.3.8 | 3-phytase |
biotechnology |
a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus |
| 3.1.3.8 | 3-phytase |
biotechnology |
the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme |
| 3.1.3.8 | 3-phytase |
biotechnology |
potential of using yeast as a phytase carrier in the gastrointestinal tract. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate (i.e. myo-inositol 1,2,3,4,5-pentakisphosphate) or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified |
| 3.1.3.8 | 3-phytase |
biotechnology |
production of phytase in laboratory-scale fermenter. Maintaining an acidic environment (pH 1.5-1.8) in the fermentation broth after the initial buildup of cell mass along with proper fragmentation of filamentous fungi results in significant improvement in phytase productivity |
| 3.1.3.8 | 3-phytase |
biotechnology |
a cross-linked enzyme aggregate (CLEA) of 3-phytase is synthesised, which is incubated with vanadate and tested as a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide as the oxidant. The results show that the 3-phytase-CLEA demonstrates a similar efficiency (ca. 95% conversion) and asymmetric induction (ca. 60%) as the free enzyme. Moreover, the 3-phytase-CLEA can be reused at least three times without significant loss of activity |
| 3.1.3.8 | 3-phytase |
biotechnology |
to evaluate the ability of EDTA to improve phytate P utilization and the possible synergistic effect between EDTA and microbial phytase an experiment is conducted using 360 Ross 308 broiler chicks. The experiment is carried out using a completely randomized design. Four replicate of 15 chicks per each are fed dietary treatments. Phytase supplementation of P-deficient diets significantly improves weight gain and feed efficiency, but it has no effect on feed consumption. Microbial phytase supplementation significantly decreases alkaline phosphatase concentration. Results obtained suggest no synergistic effect between phytase and EDTA in broiler chicks |
| 3.1.3.8 | 3-phytase |
biotechnology |
Pichia pastoris containing cell-surface phytase releases phosphorus from feedstuff at a level similar to secreted phytase |
| 3.1.3.8 | 3-phytase |
biotechnology |
synthesis of a modified phytase gene with 1256 bp in length with optimal codons for expression in Pichia pastoris. A Pichia pastoris strain that expresses the modified phytase gene phyA-mod shows a 50% increase in phytase activity level |
| 3.13.1.4 | 3-sulfinopropanoyl-CoA desulfinase |
biotechnology |
the enzyme is part of the 3,3'-dithiopropionate degradation pathway. The elucidation of this pathway and the identification of the genes could provide an strategy to engineer strains suitable for biotechnological production of polythioesters |
| 1.1.1.50 | 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) |
biotechnology |
transfection of cells with plasmids encoding a 3alpha-hydroxysteroid dehydrogenase-Del1 deposition domain fusion protein. The Del1 deposition domain immobilizes the enzyme in the extracellular matrix without interfering with its enzymatic activity. Extracellular matrix conditioned by cells transfected with 3alpha-hydroxysteroid dehydrogenase-Del1 deposition domain fusion significantly suppresses the growth of otherwise untreated LNCaP cells |
| 2.4.1.25 | 4-alpha-glucanotransferase |
biotechnology |
industrial production of cycloamylase with mutant enzyme Y54G, which shows high cyclization activity and low hydrolytic activity |
| 6.2.1.12 | 4-coumarate-CoA ligase |
biotechnology |
viability of a flavonoid network to utilize acrylic acid analogues and describe the combinatorial mutasynthesis of novel unnatural flavonoids using recombinant Saccharomyces cerevisiae, overview |
| 2.5.1.34 | 4-dimethylallyltryptophan synthase |
biotechnology |
the combination of the two dimethylallyltryptophan synthases FgaPT2 and 7-DMATS (EC 2.5.1.34 and EC 2.5.1.80) can be successfully used for chemoenzymatic synthesis of the diprenylated derivatives. The potential of recombinant enzymes from secondary metabolite biosynthesis as promising tools for the production of designed compounds is demonstrated |
| 2.4.1.152 | 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase |
biotechnology |
a baculoviral expression system of FucT-IX appears to be a promising strategy for overproduction as compared to overproduction in Escherichia coli or mammalian cells |
| 4.3.3.7 | 4-hydroxy-tetrahydrodipicolinate synthase |
biotechnology |
enzyme is a target for herbicide and anti-microbial action |
| 4.1.1.61 | 4-hydroxybenzoate decarboxylase |
biotechnology |
use of enzyme for conversion of phenol into 4-hydroxybenzoic acid |
| 1.14.14.37 | 4-hydroxyphenylacetaldehyde oxime monooxygenase |
biotechnology |
engineering of the dhurrin pathway from Sorghum bicolor into the chloroplasts of Nicotiana tabacum. The entire pathway can be introduced into the chloroplast by integrating membrane-bound cytochrome P450 enzymes CYP79A1, CYP71E1, and soluble glucosyltransferase UGT85B1 into a neutral site of the Nicotiana tabacum chloroplast genome. The two P450s and the UGT85B1 are functional when expressed in the chloroplasts and convert endogenous tyrosine into dhurrin using electrons derived directly from the photosynthetic electron transport chain, without the need for the presence of an NADPH-dependent P450 oxidoreductase. The dhurrin produced in the engineered plants amounts to 0.1-0.2% of leaf dry weight compared to 6% in sorghum |
| 1.14.14.37 | 4-hydroxyphenylacetaldehyde oxime monooxygenase |
biotechnology |
in vitro reconstitution of the entire dhurrin biosynthetic pathway from tyrosine is accomplished by the insertion of CYP79 (tyrosine N-hydroxylase), P450ox, and NADPH-P450 oxidoreductase in lipid micelles in the presence of uridine diphosphate glucose glucosyltransferase |
| 3.1.3.26 | 4-phytase |
biotechnology |
a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus |
| 3.1.3.26 | 4-phytase |
biotechnology |
the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme |
| 3.1.3.26 | 4-phytase |
biotechnology |
potential of using yeast as a phytase carrier in the gastrointestinal tract. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified |
| 3.1.3.26 | 4-phytase |
biotechnology |
production of phytase in laboratory-scale fermenter. Maintaining an acidic environment (pH 1.5-1.8) in the fermentation broth after the initial buildup of cell mass along with proper fragmentation of filamentous fungi results in significant improvement in phytase productivity |
| 3.1.3.26 | 4-phytase |
biotechnology |
high levels of stable phytase is expressed in the culture medium of transgenic Medicago truncatula cell suspension cultures |
| 3.1.3.26 | 4-phytase |
biotechnology |
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement |
| 3.1.3.26 | 4-phytase |
biotechnology |
phytase from Bacillus subtilis (168phyA) is constitutively expressed in tobacco and Arabidopsis to generate transgenic plants capable of utilizing exogenous phytate. In tobacco, phytase activities in transgenic leaf and root extracts are seven to eight times higher than those in wild-type extracts; whereas, the extracellular phytase activities of transgenic plants are enhanced by four to six times. Similar results are observed from the transgenic Arabidopsis. These results may offer a new perspective on mobilizing soil phytate into inorganic phosphate for plant uptake |
| 3.1.3.26 | 4-phytase |
biotechnology |
phytase from Bacillus subtilis is introduced into the cytoplasm of tobacco cells that results in equilibrium shift of inositol biosynthesis pathway, thereby making more phosphate available for primary metabolism. The transgenic line exhibit phenotypic changes like increased flowering, lower seed IP6/IP5 ratio, and enhanced growth under phosphate starvation conditions compared to wild type |
| 3.1.3.26 | 4-phytase |
biotechnology |
phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract |
| 3.1.3.26 | 4-phytase |
biotechnology |
ten bean cultivars are evaluated for variability in phytate, phenolic, and mineral contents, phytase activity, and antioxidant properties to elucidate the relationship of these components. Multivariate data analysis performed on 22 components analyzed in this study using principal component analysis and cluster methods demonstrate that differences in phytase, antioxidant activity, mineral contents, and bioavailability are much larger within market class than among bean cultivars |
| 3.1.3.26 | 4-phytase |
biotechnology |
Yersinia rohdei phytase is an attractive additive to animal feed |
| 1.1.3.47 | 5-(hydroxymethyl)furfural oxidase |
biotechnology |
development of a facile gene shuffling approach to rapidly combine stabilizing mutations in a one-pot reaction. This allows the identification of the optimal combination of several beneficial mutations. The approach quickly discriminates stable and active multi-site variants, making it a very useful addition to FRESCO (framework for rapid enzyme stabilization by computational libraries) method |
| 2.3.1.37 | 5-aminolevulinate synthase |
biotechnology |
Propionibacterium acidipropionici TISTR442 produce the highest amount of 5-aminolevulinic acid (ALA) when cultivated in medium supplemented with glycine at 18 g/l. This optimal condition for ALA production via the addition of glycine provides an easy and low-cost technique for themass cultivation of Propionibacterium acidipropionici |
| 2.5.1.78 | 6,7-dimethyl-8-ribityllumazine synthase |
biotechnology |
a circularly permuted variant of lumazine synthase affords versatile building blocks for the construction of nanocompartments that can be easily produced, tailored, and diversified. The topologically altered protein self-assembles into spherical and tubular cage structures with morphologies that can be controlled by the length of the linker connecting the native termini. Permutated lumazine synthase proteins integrate into wild-type and other engineered lumazine synthase assemblies by coproduction in Escherichia coli to form patchwork cages. This coassembly strategy enables encapsulation of guest proteins in the lumen, modification of the exterior through genetic fusion, and tuning of the size and electrostatics of the compartments |
| 2.5.1.78 | 6,7-dimethyl-8-ribityllumazine synthase |
biotechnology |
the C-terminal tail of ribiflavin synthase can act as an encapsulation tag capable of targeting other proteins to the lumazine synthase capsid interior. Fusion of to either the last 11 or the last 32 amino acids of riboflavin synthase, yields variant GFP11 or GFP32, respectively. After purification, lumazine synthase capsids that have been coproduced in bacteria with GFP11 and GFP32 are 15- and 6fold more fluorescent, respectively. GFP11 is localized within the lumazine synthase capsid. Fusing the last 11 amino acids of riboflavin synthase to the C-terminus of the Abrin A chain also leads to its encapsulation by lumazine synthase at a level similar to that of GFP11. Mild changes in pH and buffer identity trigger dissociation of the GFP11 guest |
| 2.3.1.94 | 6-deoxyerythronolide-B synthase |
biotechnology |
a derivative of Escherichia coli is genetically engineered to produce 6-deoxyerythronolide B, the macrocyclic core of the antibiotic erythromycin |
| 2.3.1.94 | 6-deoxyerythronolide-B synthase |
biotechnology |
a new Escherichia coli stain, YW9, is created, featuring a plasmid-free heterologous pathway for the production of the polyketide product 6-deoxyerythronolide B |
| 2.3.1.94 | 6-deoxyerythronolide-B synthase |
biotechnology |
polyketide synthases synthesize the polyketide cores of biologically active compounds, including natural products that have become important pharmaceuticals, like erythromycin |
| 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 |
| 2.3.1.165 | 6-methylsalicylic-acid synthase |
biotechnology |
production of unnatural polyketides e.g. 4-hydroxy-6-methyl-2-pyrone in E. coli and yeast after heterologous expression of the enzyme |
| 2.3.1.165 | 6-methylsalicylic-acid synthase |
biotechnology |
functional heterologous expression of enzyme requires the presence of a 4-phosphoantetheinyl transferase for activation. Coexpression of both enzymes results in production of 6-methylsalicylic acid in good yields |
| 2.3.1.165 | 6-methylsalicylic-acid synthase |
biotechnology |
polyketides are a group of natural products that have gained much interest due to their use as antibiotics, cholesterol lowering agents, immunosuppressors and other drugs, it is therefor of general interest to transfer polyketide synthase genes into heterologous hosts that can overproduce the corresponding polyketides |
| 2.3.1.165 | 6-methylsalicylic-acid synthase |
biotechnology |
production of 6-methylsalicylic acid which is used as human pharmaceutical |
| 2.3.1.165 | 6-methylsalicylic-acid synthase |
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 |
| 2.7.1.11 | 6-phosphofructokinase |
biotechnology |
design of strains with improved antibiotic production |
| 2.5.1.80 | 7-dimethylallyltryptophan synthase |
biotechnology |
the combination of the two dimethylallyltryptophan synthases FgaPT2 and 7-DMATS (EC 2.5.1.34 and EC 2.5.1.80) can be successfully used for chemoenzymatic synthesis of the diprenylated derivatives. The potential of recombinant enzymes from secondary metabolite biosynthesis as promising tools for the production of designed compounds is demonstrated |
| 1.1.1.36 | acetoacetyl-CoA reductase |
biotechnology |
construction an evaluation of a polyhydroxybutyrate production system using Zea mays chloroplasts expressing the enzyme from Alcaligenes eutrophus |
| 2.3.1.194 | acetoacetyl-CoA synthase |
biotechnology |
the enzyme represents a potential target to increase the flux through the mevalonate pathway |
| 2.2.1.6 | acetolactate synthase |
biotechnology |
construction of a vector system for chloroplast transformation with acetolactate synthase, generation of a series of Arabidopsis thaliana mutated acetolactate synthase genes and introduction of constructs with the aminoglycoside 3'-adenyltransferase gene into the Nicotiana tabacum chloroplast genome by particle bombardment |
| 2.2.1.6 | acetolactate synthase |
biotechnology |
the reaction specificity of acetolactate synthase from Thermus thermophilus can be redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. Quadruple mutant Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type mainly because of H474R amino acid substitution, which likely generates two new hydrogen bonds near the thiamine diphosphate-binding site |
| 6.4.1.2 | acetyl-CoA carboxylase |
biotechnology |
the enzyme is a target for development of herbicides |
| 3.1.1.7 | acetylcholinesterase |
biotechnology |
enzyme immobilised on a nanostructured Langmuir-Blodgett proteo-glycolipidic bilayer, directly interfaced with an efficient optical device. Direct investigation of the kinetic behaviour of enzyme |
| 2.6.1.11 | acetylornithine transaminase |
biotechnology |
the pCR2.1-argD complementation plasmid is stably maintained in the argD(1000)::Tn5 transposon mutant growing in host tissues without any antibiotic selection. The pCR2.1-argD complementation plasmid can be useful for the expression of genes, markers, and reporters in Erwinia amylovora growing in planta, without concern about losing the plasmid over time |
| 3.1.3.2 | acid phosphatase |
biotechnology |
immobilization of the purified enzyme on glutaraldehyde-activated aminopropyl controlled-pore glass activates the enzyme, assay automatization, system evaluation, overview |
| 3.1.3.2 | acid phosphatase |
biotechnology |
improved stability and catalytic kinetics of acid phosphatase immobilized on composite beads of chitosan and activated clay as a model system for enzyme immobilization optimization |
| 3.1.3.2 | acid phosphatase |
biotechnology |
improvement of enzymic reaction by intercalated clay surfaces with free and immobilized enzyme, overview |
| 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 |
| 3.4.22.14 | actinidain |
biotechnology |
actinidin might be utilized to eliminate the milk fat globule membranes (MFGM) protein residues from cream and its derivatives |
| 3.5.1.70 | aculeacin-A deacylase |
biotechnology |
recombinant enzyme covalently immobilized onto several epoxy-activated supports in order to obtain a robust biocatalyst to be used in industrial bioreactors. The best biocatalyst is obtained by attaching the enzyme on Sepabeads EC-EP5 |
| 1.3.1.8 | acyl-CoA dehydrogenase (NADP+) |
biotechnology |
optimization of oil-based extended fermentation of recombinant Streptomyces cinnamonensis, expressing the enzyme from Streptomyces collinus, is used to provide methylmalonyl-CoA precursors for monensin biosynthesis, overview |
| 3.1.2.20 | acyl-CoA hydrolase |
biotechnology |
enzyme is involved in fatty acid biosynthesis and may be a good target for improvement of special oil production in transgenic plants |
| 1.3.3.6 | acyl-CoA oxidase |
biotechnology |
potential depolluting agent by degradation of oils |
| 1.3.3.6 | acyl-CoA oxidase |
biotechnology |
several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids |
| 3.5.1.97 | acyl-homoserine-lactone acylase |
biotechnology |
the enzyme can be used in quenching quorum sensing |
