EC Number   |
Recommended Name |
Application |
|---|
    1.2.1.11 | aspartate-semialdehyde dehydrogenase |
biotechnology |
the modofied enzyme with altered substrate specificity using NAD(H) is preferred in biotechnological production of amino acids due to lower costs and higher stability |
| 1.2.1.12 | glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) |
biotechnology |
molecular evolution or metabolic engineering protocols can exploit substrate channeling of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and L-lactate dehydrogenase (LDH) for metabolic flux control by fine-tuning substrate-binding affinity for the key enzymes in the competing reaction paths |
| 1.2.1.44 | cinnamoyl-CoA reductase |
biotechnology |
CCR downregulation may become a successful strategy to improve biomass processing if the variability in down-regulation and the yield penalty can be overcome |
| 1.2.1.44 | cinnamoyl-CoA reductase |
biotechnology |
potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants |
| 1.2.1.46 | formaldehyde dehydrogenase |
biotechnology |
development of novel formaldehyde-selective amperometric biosensors based on immobilized NAD+- and glutathione dependent formaldehyde dehydrogenase with high selectivity to formaldehyde and a low cross-sensitivity to other substances, the laboratory prototype of the sensor is applied for FA testing in some real samples of pharmaceutical (formidron), disinfectant (descoton forte) and industrial product (formalin) |
| 1.2.1.50 | long-chain acyl-protein thioester reductase |
biotechnology |
production of jojoba plant wax esters |
| 1.2.1.67 | vanillin dehydrogenase |
biotechnology |
Amycolatopsis sp. ATCC 39116 vdh mutant represents an optimized and industrially applicable platform for biotechnological production of natural vanillin |
| 1.2.1.68 | coniferyl-aldehyde dehydrogenase |
biotechnology |
biotransformation of eugenol to ferulic acid by a recombinant strain of Ralstonia eutropha H16. The gene calB, encoding coniferyl aldehyde dehydrogenase, and ehyAB and calA encoding eugenol hydroxylase and coniferyl alcohol dehydrogenase, respectively, are amplified and combined to construct a catabolic gene cassette. This gene cassette is cloned in the broad-host-range vector pBBR1-JO2 and transferred to Ralstonia eutropha H16. A recombinant strain of Ralstonia eutropha H16 harboring this plasmid expresses functionally active eugenol hydroxylase, coniferyl alcohol dehydrogenase, and coniferyl aldehyde dehydrogenase. Cells of Ralstonia eutropha H16 from the late-exponential growth phase are used asa biocatalysts for the biotransformation of eugenol to ferulic acid. A maximum conversion rate of 2.9 mM of eugenol per h per liter of culture is achieved with a yield of 93.8 mol% of ferulic acid from eugenol within 20 h, without further optimization |
| 1.2.1.68 | coniferyl-aldehyde dehydrogenase |
biotechnology |
highly efficient two-step biotransformation of eugenol to ferulic acid and further conversion to vanillin in recombinant strains of Escherichia coli. Maximum production rate for ferulic acid at large scale is 14.4 mM per h per liter of culture, yield of 93.3% with respect to the added amount of eugenol |
| 1.2.1.70 | glutamyl-tRNA reductase |
biotechnology |
recombinant Escherichia coli allows efficient production of 5-aminolevulinic acid directly from glucose |
| 1.2.1.75 | malonyl-CoA reductase (malonate semialdehyde-forming) |
biotechnology |
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production |
| 1.2.4.1 | pyruvate dehydrogenase (acetyl-transferring) |
biotechnology |
active expression of enzyme from non-halophilic Zymomonas mobilis in the haloarchaeon Haloferax volcanii with no difference in the secondary structure. Post-transcriptional mechanisms in the stationary phase appear to limit the amount of recombinant protein expressed |
| 1.2.7.1 | pyruvate synthase |
biotechnology |
pyruvate:ferredoxin oxidoreductase PFR1 and [Fe-Fe]-hydrogenase HYDA1 of Chlamydomonas can be coupled for pyruvate-dependent H2 production |
| 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 |
| 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 |
| 1.3.1.32 | maleylacetate reductase |
biotechnology |
Sphingobium chlorophenolicum has assembled new catabolic pathways to degrade pentachlorophenol and use the ring-cleavage products as their carbon sources |
| 1.3.3.5 | bilirubin oxidase |
biotechnology |
the enzyme functions effectively as the biocathode of a H2/O2 biofuel cell. It is immmobilized as a multiple layer in a cationic polymer (poly-L-lysine) matrix on an electrode surface. The BOD-modified electrode catalyzes four-electron reduction of O2 to water without any mediator, to produce a diffusion-controlled voltammogram for the O2 reduction in a quiescent solution. Construction of such a multiple enzyme layer is useful for increasing the current density even in direct electron transfer-type bioelectrocatalysis |
| 1.3.3.5 | bilirubin oxidase |
biotechnology |
the wired" enzyme is superior to pure platinum as a electrocatalyst of the four-electron electroreduction of O2 to water. The "wired" bilirubin oxidase-coated carbon cathode operates for more than 1 week at 37°C in a glucose-containing physiological buffer solution. Key application would be in a glucose-O2 biofuel cell. The cathode is short-lived in serum, losing its electrocatalytic activity in a few hours. The damaging serum component is a product of the reaction of urate and dissolved oxygen. Exclusion of urate, by application of Nafion(TM) film in the cathode, improves the stability in serum |
| 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 |
| 1.3.3.11 | pyrroloquinoline-quinone synthase |
biotechnology |
cofactor engineering of PQQ in Gluconobacter oxydans is beneficial for enhancing the production of quinoprotein-related products |
| 1.3.5.1 | succinate dehydrogenase |
biotechnology |
a new host-vector system for Mortierella alpina 1S-4, zygomycetes, on the basis of self-cloning for the industrial application of Mortierella transformants is developed. Transformants expressing the Escherichia coli uidA gene encoding beta-glucuronidase by using the mutant H243L as the selectable marker (leading to to carboxin resistance) |
| 1.3.7.4 | phytochromobilin:ferredoxin oxidoreductase |
biotechnology |
transposon-based directed tagging strategy using maize Ds element generates a wide diversity of tagged and non-tagged alleles that can be used to generate allelic series or deletion of clustered genes |
| 1.3.7.4 | phytochromobilin:ferredoxin oxidoreductase |
biotechnology |
the flooding (rf) mutation identified may provide a target for biotechnological renovation of tomato germplasm in future breeding |
| 1.4.1.1 | alanine dehydrogenase |
biotechnology |
heterologous expression of the Bacillus subtilis AlaDH in Lactococcus lactis using the promoter of lactate dehydrogenase from Streptococcus thermophilus leads to a better alanine production in the recombinant strain |
| 1.4.1.2 | glutamate dehydrogenase |
biotechnology |
a strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibit faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Flocculation of both Y and Y-5 can be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation is promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. This opens up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing |
| 1.4.1.2 | glutamate dehydrogenase |
biotechnology |
method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization |
| 1.4.1.2 | glutamate dehydrogenase |
biotechnology |
the rate of flocculation is promoted by a-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing |
| 1.4.1.4 | glutamate dehydrogenase (NADP+) |
biotechnology |
enzyme TrGDH is a promising candidate gene for maintaining or improving yields in crop plants via genetic engineering |
| 1.4.1.9 | leucine dehydrogenase |
biotechnology |
an efficient stereospecific enzymatic synthesis of L-valine, L-leucine, L-norvaline, L-norleucine and L-isoleucine from the corresponding alpha-keto acids by coupling the reactions catalysed by leucine dehydrogenase and glucose dehydrogenase/galactose mutarotase. Giving high yields of L-amino acids, the procedure is economical and easy to perform and to monitor at a synthetically useful scale (1-10 g) |
| 1.4.1.16 | diaminopimelate dehydrogenase |
biotechnology |
high thermostability and relaxed substrate profile of Symbiobacterium thermophilum meso-DAPDH warrant it as an excellent starting enzyme for creating effective D-amino acid dehydrogenases by protein engineering |
| 1.4.1.20 | phenylalanine dehydrogenase |
biotechnology |
application of the immobilised mutant enzyme N145A that is remarkably robust, even in the presence of high concentrations of polar or non-polar organic solvents such as acetone, methanol, n-hexane, toluene and methylene chloride in the synthesis of p-NO2-phenylalanine from the poorly water-soluble p-NO2-phenylpyruvic acid. 100% stereoselectivity |
| 1.4.1.20 | phenylalanine dehydrogenase |
biotechnology |
use of fed-batch cultivation for achieving high cell densities for the pilot-scale production of the recombinant phenylalanine dehydrogenase |
| 1.4.3.3 | D-amino-acid oxidase |
biotechnology |
DAAO can be used to synthesize cephalosporin antibiotics |
| 1.4.3.3 | D-amino-acid oxidase |
biotechnology |
the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment |
| 1.4.3.3 | D-amino-acid oxidase |
biotechnology |
the enzyme is used as a biocatalyst in cephalosporin C conversion on industrial scale |
| 1.4.3.10 | putrescine oxidase |
biotechnology |
potential of putrescine oxidase for the bioproduction of N-heterocycles from cadaverine. Complete biotransformation of cadaverine is observed in whole cells at physiological conditions |
| 1.4.3.11 | L-glutamate oxidase |
biotechnology |
an amperometric microbiosensor for real time monitoring L-glutamate release in neural tissue, based on enzymatic oxidation catalyzed by the L-glutamate oxidase is developed. By means of a sol-gel coating method, L-glutamate oxidase is entrapped in a biocompatible gel layer that provides a benign environment and retains enzyme activity on the surface of Pt microelectrode. Prior to gel layer formation, a modification on the surface of Pt microelectrode with poly(phenylene diamine) enables the microbiosensor screen majority of common potential interfering substances existing in physiological samples. The resulting L-glutamate microbiosensors are characterized by a fast response, high sensitivity, favourable selectivity and excellent long-term stability |
| 1.4.3.11 | L-glutamate oxidase |
biotechnology |
application of L-glutamate oxidase with catalase (KatE) to whole-cell systems for glutaric acid production in Escherichia coli. The 2-oxoglutarate regeneration system has potential for improving production in various aminotransferase systems |
| 1.4.3.11 | L-glutamate oxidase |
biotechnology |
engineering of L-glutamate oxidase has great potentials to enhance the industrial production of 2-oxoglutarate. A whole-cell biocatalyst for 2-oxoglutarate production is developed by co-expression of both S280T/H533L mutant and KatE catalase. S280T/H533L mutant has high maximal velocity (Vmax: 0.2313 mM/mg/min) and the low Km-value of 2.7 mM. Randomized ribosome binding site (RBS) sequences are introduced to generate vectors with varying expression levels of S280T/H533L and KatE, and two optimized coexpression strains are obtained after screening. The 2-oxoglutarate production reaches a maximum titer of 181.9 g/l after 12 h conversation using the optimized whole-cell biocatalyst, with a molar conversion rate of substrate higher than 86.3% in the absence of exogenous catalase, while the molar conversion rate of substrate using the wild-type biocatalyst is less than 30% |
| 1.4.3.11 | L-glutamate oxidase |
biotechnology |
to simplify technological processes and reduce production costs, cascade biocatalysis for 2-oxoglutarate production is constructed by simultaneously expressing L-glutamate oxidase (LGOX) from Streptomyces viridosporus and KatG from Escherichia coli W3110 in Escherichia coli BL21 (DE3). In vivo cascade biocatalysis is constructed and optimized by promoter engineering to finely control the coexpression of LGOX and KatG, thus resulting in a significant increase in 2-oxoglutarate concentration and its conversion rate with no catalase addition |
| 1.4.3.16 | L-aspartate oxidase |
biotechnology |
StLASPO represents an appropriate biocatalyst for the resolution of racemic solutions of D,L-aspartate and a well-suited protein scaffold to evolve a L-amino acid oxidase activity by protein engineering |
| 1.4.3.22 | diamine oxidase |
biotechnology |
supramolecular tandem assays exploit the dynamic binding of a fluorescent dye with a macrocyclic host in competition with the binding of the substrate and product. Two examples of enzymatic reactions were investigated: the hydrolysis of arginine to ornithine catalyzed by arginase and the oxidation of cadaverine to 5-aminopentanal by diamine oxidase, in which the substrates have a higher affinity to the macrocycle than the products (substrate-selective assays). The depletion of the substrate allows the fluorescent dye to enter the macrocycle in the course of the enzymatic reaction, which leads to the desired fluorescence response. For arginase, p-sulfonatocalix[4]arene is used as the macrocycle, and for diamine oxidase, cucurbit[7]uril (CB7) is used. An additional reporter pair, namely cucurbit[7]uril (CB7)/acridine orange (AO) is applied and the potential of tandem assays for inhibitor screening is demonstrated |
| 1.5.1.3 | dihydrofolate reductase |
biotechnology |
in vivo screening system to select for functionally active proteins with increased solubility. Fusion of enzyme to green fluorescent protein as reporter for solubility |
| 1.5.1.3 | dihydrofolate reductase |
biotechnology |
method for screening combinatorial or other libraries of enzyme based on affinities of the inhibitors with the enzyme |
| 1.5.1.3 | dihydrofolate reductase |
biotechnology |
method for screening combinatorial or other libraries of Plasmodium falciparum enzyme based on affinities of the inhibitors with the enzyme |
| 1.5.1.39 | FMN reductase [NAD(P)H] |
biotechnology |
enzyme-catalyzed cofactor regeneration is a significant approach to avoid large quantities consumption of oxidized cofactor, which is vital in a variety of bioconversion reactions. NADH: FMN oxidoreductase is an ideal regenerating enzyme because innocuous molecular oxygen is required as an oxidant. But the by-product H2O2 limits its further applications at the industrial scale, therefore, mutants with improved features are constructed |
| 1.6.1.1 | NAD(P)+ transhydrogenase (Si-specific) |
biotechnology |
enzymatic NADH production system in reverse micelles using a bacterial glycerol dehydrogenase. The present system is further extended to NADPH production in reverse micelles by coupling with a bacterial soluble transhydrogenase that catalyses the conversion of NADP+ to NADPH using NADH. Glycerol dehydrogenase and soluble transhydrogenase have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media |
| 1.6.1.1 | NAD(P)+ transhydrogenase (Si-specific) |
biotechnology |
Escherichia coli strain is transformed with a two plasmid system, one encoding the udhA gene and the other one encoding the phb operon. The functionality of this particular system is successfully demonstrated in PHB production experiments. Both productivity and yield of PHB can be increased when NADPH availability is increased |
| 1.6.2.4 | NADPH-hemoprotein reductase |
biotechnology |
the enzyme is displayed on the cell surface of Escherichia coli, creating a whole-cell biocatalyst for oxidoreduction of various substrates |
| 1.6.5.2 | NAD(P)H dehydrogenase (quinone) |
biotechnology |
the flavoprotein WrbA from Escherichia coli represents a new family of multimeric flavodoxin-like proteins implicated in cell protection against oxidative stress, WrbA has NAD(P)H: quinone reductase activity, forms multimers and binds FMN only weakly |
| 1.8.3.7 | formylglycine-generating enzyme |
biotechnology |
bioconjugation chemistry, formylglycine-generating enzymes catalyze the site-specific oxidation of a cysteine residue to the aldehyde-containing amino acid Ca-formylglycine (FGly). This noncanonical residue can be generated within any desired target protein and can subsequently be used for bioorthogonal conjugation reactions |
| 1.8.3.7 | formylglycine-generating enzyme |
biotechnology |
site-specific bioconjugation. Formylglycine-generating enzymes allow to posttranslationally introduce the amino acid Calpha-formylglycine (FGly) into recombinant proteins, starting from cysteine or serine residues within distinct consensus motifs |
| 1.8.3.7 | formylglycine-generating enzyme |
biotechnology |
site-specific conjugation strategy for dual antibody-drug conjugates using aerobic formylglycine-generating enzymes |
| 1.8.3.7 | formylglycine-generating enzyme |
biotechnology |
the enzyme is an enabling biotechnology tool due to the robust utility of the aldehyde product as a bioconjugation handle in recombinant proteins |
| 1.8.4.11 | peptide-methionine (S)-S-oxide reductase |
biotechnology |
enzyme is a target for modification of redox-dependent regulation |
| 1.8.4.12 | peptide-methionine (R)-S-oxide reductase |
biotechnology |
enzyme is a target for modification of redox-dependent regulation |
| 1.10.3.2 | laccase |
biotechnology |
expression of non-fused enzyme and hydrophobin-enzyme fusion protein in Trichoderma reesei, intracellular accumulation and degradation of fusion protein, production of non-fused enzyme at up to 920 mg per l of fed-batch culture, purification from culture supernatant |
| 1.10.3.2 | laccase |
biotechnology |
five SvLAC genes (SvLAC9, SvLAC13, SvLAC15, SvLAC50, and SvLAC52) fulfill the criteria established to identify lignin-related candidates. They are strong candidates to be involved in lignin polymerization in Setaria viridis and might be good targets for lignin bioengineering strategies |
| 1.10.3.2 | laccase |
biotechnology |
robust catalytic efficiency in the presence of organic solvents suggest its industrial and biotechnological application potentials for the sustainable development of green chemistry |
| 1.10.3.2 | laccase |
biotechnology |
the purified enzyme displays greater efficiency in Remazol Brilliant Blue R decolourization (90%) in absence of redox mediator, an important property for biotechnological applications |
| 1.11.1.5 | cytochrome-c peroxidase |
biotechnology |
cytochrome c peroxidase as a platform to develop specific peroxygenation catalysts |
| 1.11.1.6 | catalase |
biotechnology |
development of simple methods for production and purification of catalases, determination of adsorption capacity and effects upon binding on enzyme activity of different minerals, binding capacities and activities at different pH/pI, one of the most promising adsorbent is hydroxylapatite, overview |
| 1.11.1.6 | catalase |
biotechnology |
wheat grass detoxifying substance in production or cultivation of Paramecium on wheat grass powder inoculated with Klebsiella pneumoniae |
| 1.11.1.10 | chloride peroxidase |
biotechnology |
CPO is used as a versatile biological catalyst |
| 1.11.1.13 | manganese peroxidase |
biotechnology |
biotechnological applications require large amounts of low-cost enzymes, one of the appropriate approaches for this is to utilize the potential of lignocellulosic wastes, some of which may contain significant concentrations of soluble carbohydrates and inducers of enzyme synthesis, ensuring efficient production of ligninolytic enzymes |
| 1.11.1.14 | lignin peroxidase |
biotechnology |
Pleurotus ostreatus is a good candidate for scale-up ligninolytic enzyme production |
| 1.12.7.2 | ferredoxin hydrogenase |
biotechnology |
practical application in solar energy bioconversion |
| 1.13.11.1 | catechol 1,2-dioxygenase |
biotechnology |
product is precursor of the industrially important compound adipic acid |
| 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 |
| 1.13.11.12 | linoleate 13S-lipoxygenase |
biotechnology |
the tomloxD gene encoding the enzyme has potential applications in engineering cropping plants that are resistant to biotic and/or abiotic stress factors |
| 1.13.11.49 | chlorite O2-lyase |
biotechnology |
degradation of benzene from anoxic polluted soil with chlorate |
| 1.13.12.2 | lysine 2-monooxygenase |
biotechnology |
immobilization of L-lysine-2-monooxygenase on an electrode surface, via polymerization of polyvinyl alcohol, provides a biosensor that detects L-lysine concentrations down to 0.01 mM |
| 1.13.12.2 | lysine 2-monooxygenase |
biotechnology |
immobilization on silica gel provides a flow-through analyzer for concentrations between 5.5 and 55 mM L-lysine at pH 8.2, it retains 50% activity after two months |
| 1.13.12.5 | Renilla-type luciferase |
biotechnology |
expression of native gene and commercial synthetic gene, optimized for expression, in several cell lines and in mouse. Use of synthetic gene as primary reporter gene with high sensitivity in living rodents |
| 1.13.12.5 | Renilla-type luciferase |
biotechnology |
use of enzyme as a reporter is dependent on the promotor driving its expression, the presence of co-transfected transgenes, and the androgen responsiveness of the cell line used |
| 1.13.12.5 | Renilla-type luciferase |
biotechnology |
use of native coelenterazine and its derivatives e, -f, -h, as substrates for use in cell culture and living animals |
| 1.13.12.5 | Renilla-type luciferase |
biotechnology |
popular reporter enzyme for gene expression and biosensor applications |
| 1.13.12.5 | Renilla-type luciferase |
biotechnology |
split luciferase complementation is applied to study dynamic protein-protein interactions in live bacteria. Nonspecific inhibition of Rluc activity by small molecule effectors compromises the utility of this technique in measuring dynamic protein-protein interactions |
| 1.13.12.5 | Renilla-type luciferase |
biotechnology |
an advanced Fc-binding probe, FcUni-RLuc, is produced and functionally assayed for labelling IgGs. The Fc antibody binding sequence HWRGWV is fused to Renilla luciferase, and the purified probe is employed for bioluminescence enzyme-linked immunoabsorbance assay of Her2 positive cells |
| 1.13.12.6 | Cypridina-luciferin 2-monooxygenase |
biotechnology |
use of enzyme as a potent secreted reporter |
| 1.13.12.7 | firefly luciferase |
biotechnology |
imaging technology |
| 1.13.12.7 | firefly luciferase |
biotechnology |
molecular biology studies with luciferase as reproter gene, bioimaging |
| 1.13.12.7 | firefly luciferase |
biotechnology |
extensive and advantageous application of this enzyme in biotechnology is restricted due to its low thermal stability |
| 1.13.12.18 | dinoflagellate luciferase |
biotechnology |
the dinoflagellate luciferase gene is an efficient marker of gene expression in mammalian cells |
| 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 |
| 1.14.11.17 | taurine dioxygenase |
biotechnology |
model system for non-heme iron oxygenases |
| 1.14.11.26 | deacetoxycephalosporin-C hydroxylase |
biotechnology |
production of beta-lactam antibiotics |
| 1.14.11.66 | [histone H3]-trimethyl-L-lysine9 demethylase |
biotechnology |
continual removal of H3K9 promoter methylation by Jmjd2 demethylases represents a novel mechanism ensuring transcriptional competence and stability of the pluripotent cell identity |
| 1.14.13.22 | cyclohexanone monooxygenase |
biotechnology |
biocatalysis system for Baeyer-Villiger oxidations, the average specific oxidation rate and product molar yield based on reaction substrate reaches 0.15 g/g dry cells/h (21.9 micromol/min/g of dry cells), at high cell densities (20 g dry cells/l) the specific product formation rate is lower with 0.12 g/g dry cells/h and 17.5 micromol/min/g of dry cells (probably due to low availability of the energy source glucose), though absolute yield is 2fold higher |
| 1.14.13.25 | methane monooxygenase (soluble) |
biotechnology |
high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs |
| 1.14.13.25 | methane monooxygenase (soluble) |
biotechnology |
high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs. Poly-beta-hydroxybutyrate content of strain OB3b can reach the highest level in the shortest time as compared to other methanotrophs. Nutrients deficiency condition is beneficial for strain IMV3011 to synthesize PHB whereas it is not beneficial for other strains |
| 1.14.13.25 | methane monooxygenase (soluble) |
biotechnology |
methanol can be employed to produce large amounts of Methylosinus trichosporium biomass containing sMMO. Enzyme expression can be maintained during growth on methanol which may aid in the development of sMMO-based industrial and environmental processes |
| 1.14.13.25 | methane monooxygenase (soluble) |
biotechnology |
method by which sMMO can be produced by strain OB3b while growing on methanol in copper-containing medium |
| 1.14.13.146 | taxoid 14beta-hydroxylase |
biotechnology |
an antisense suppression approach, repressing the expression of the taxoid 14beta-hydroxlyase gene in yew cell cultures, is useful to inhibit the expression of other important genes in side-route of Taxol pathway and this may diverts the flow of taxadiene mainly towards Taxol |
| 1.14.13.231 | tetracycline 11a-monooxygenase |
biotechnology |
protocol for the nuclear transformation of Chlamydomonas reinhardtii using tetX as a selectable marker that confers stable resistance to tetracycline up to 100 microg/ml. TetX may be used to transform Chlamydomonas reinhardtii chloroplasts, related microalgae and other aerobic organisms sensitive to any tetracycline antibiotic |
| 1.14.14.1 | unspecific monooxygenase |
biotechnology |
cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants |
| 1.14.14.1 | unspecific monooxygenase |
biotechnology |
EUI and the GA metabolism pathway are useful targets for increasing the agronomic value of crops |
| 1.14.14.1 | unspecific monooxygenase |
biotechnology |
enzymatic activity of P450SMO makes it an attractive biocatalyst for asymmetric synthesis of enantiopure sulfoxides |
