EC Number   |
Recommended Name |
Application |
|---|
   1.11.1.13 | manganese peroxidase |
environmental protection |
- |
| 1.3.1.42 | 12-oxophytodienoate reductase |
environmental protection |
2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
environmental protection |
2,4-dichlorophenoxy acetic acid (2,4-D) is of particular concern, as this synthetic auxin has been the most utilized herbicide in the past 50 years. It is prevalent in agricultural fields and has been widely applied in cereal crops to control broadleaved weeds. It inhibits the growth of leaf weeds by accumulating in the plant root. 2,4-D accumulated crops, on consumption, result in gastrointestinal haemorrhage, direct myocardial toxicity, CNS depression, renal failure, and other disorders. The bacterium Bacillus licheniformis strain SL10 finds potential application in the remediation of 2,4-dichlorophenol |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
a high and sustainable lignin peroxidase activity is achieved via in situ release of H2O2 by a co-immobilized glucose oxidase. The present co-immobilization system is demonstrated to be very effective for lignin peroxidase mediated dye decolourization |
 4.99.1.2 | alkylmercury lyase |
environmental protection |
a new transgenic tobacco plant for phytoremediation of CH3Hg+ pollution: The new ppk/merT/merB-transgenic tobacco plant, which contains the integrated bacterial merB gene encoding MerB, has the ability to tolerate and accumulate high levels of Hg2+ inside the plant cells from simulated soils, probably via a chelation mechanism of polyP with Hg2+, without releasing mercury vapor into the atmosphere |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
A recombinant whole-cell bacterial sensor for highly selective and sensitive detection of bioavailable methylmercury in the environment is constructed. The biosensor carries luciferase gene as a reporter under control of a very selective Hg2+-inducible part of the mer-operon from Pseudomonas K-62 plasmid pMR26. A merB gene encoding organomercurial lyase which cleaves the C-Hg bond of methylmercury to give Hg2+ is coexpressed in the sensor. |
| 1.14.13.245 | assimilatory dimethylsulfide S-monooxygenase |
environmental protection |
Acinetobacter sp. 20B grown on dimethyl sulfide degrades up to 25% of 1.5 mg trichloroethylene/l, respectively. Escherichia coli harboring the DMS monooxygenase genes from strain 20B alone, or in combination with the cumene dioxygenase genes from Pseudomonas fluorescens IP01, degrades up to 50% and 88% of 75 mg TCE/l, respectively. The growth rates of the E. coli recombinants remain nearly unaffected by TCE at least up to 150 mg/l |
| 4.2.2.2 | pectate lyase |
environmental protection |
alkaline pectate lyases play an important role in mild and eco-friendly bioscouring pretreatment processes in the textile industry. So far, only a few pectate lyases can be applied in industrial-scale production, and many of them exhibit high production cost, low activity, and/or do not meet the treatment requirements. Recombinant PelB has with promising properties for use in bioscouring in the textile pretreatment process and is a potential enzyme for industrial applications |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
amino modified magnetic halloysite nanotube supporting chloroperoxidase immobilization is useful for enhanced stability, reusability, and efficient degradation of pesticide residue in wastewater. Degradation of mesotrione in wastewater by the immobilized CPO |
| 1.8.5.4 | bacterial sulfide:quinone reductase |
environmental protection |
anaerobic treatment of sulphate rich wastewater results in high amount of sulfide in liquid phase and gaseous phase. Sulfide is malodorous in gaseous phase and toxic even at very low concentrations in liquid phase and causes objectionable environmental issues. Sulfide present in the up-flow anaerobic sludge blanket (UASB)-treated post tanning wastewater is oxidized into elemental sulfur using sulfide:quinone oxidoreductase (SQR) immobilized on functionalized carbon-silica matrix (FCSM) in a packed bed reactor. Optimum conditions for immobilization of SQR onto FCSM are pH, 7.0, 40°C, and 10mg/g SQR during 240 min. The immobilization of SQR onto FCSM obeys the Langmuir isotherm model. The maximum sulfide oxidation is 99% at HRT of 15 h with residual sulfide of 2.4 mg/l. The formation of elemental Sulphur is confirmed by XRD studies |
| 4.2.3.27 | isoprene synthase |
environmental protection |
analysis of in vivo isoprene emission. The in vivo rate constant of IspS obeys the Arrhenius law, with an activation energy of 42.8 kJ per mol. Steady-state isoprene emission has a significantly lower temperature optimum than IspS and higher activation energy. The reversible temperature-dependent decrease in the rate of isoprene emission between 35°C and 44°C is caused by decreases in dimethylallyl diphosphate concentration, possibly reflecting reduced pools of energetic metabolites generated in photosynthesis, particularly of ATP. Strong control of isoprene temperature responses by the dimethylallyl diphosphate pool implies that transient temperature responses under fluctuating conditions in the field are driven by initial dimethylallyl diphosphate pool size as well as temperature-dependent modifications in dimethylallyl diphosphate pool size during temperature transients |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
anthropogenic activity has converted chromium (Cr), an element found in rocks, soils, plants, and animals, into a dangerous environmental pollutant. The activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI) |
| 1.14.13.7 | phenol 2-monooxygenase (NADPH) |
environmental protection |
application for enzyme-based remediation of phenolic wastewater or in phenolic biosensor, kinetic properties. Remediation of phenols at its anthropogenic source before it enters into the environmental ecosystem. Microbial degradation has gained attention for treatment of phenols owing to its ability of complete mineralization and cost effectiveness |
| 3.1.1.74 | cutinase |
environmental protection |
application of cutinase for degradationof dihexyl phthalate in the dihexyl phthalate-contaminated environments may be possible |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
application of the immobilized mercuric reductase for continuous treatment of Hg(II)-containing water in a fixed bed reactor |
| 1.8.4.9 | adenylyl-sulfate reductase (glutathione) |
environmental protection |
APR2 can be exploited for engineering heavy metal-tolerant plants in phytoremediation |
| 1.4.3.12 | cyclohexylamine oxidase |
environmental protection |
as a potential biocatalyst, the enzyme is promising in controlling cyclohexylamine pollution and deracemization of chiral amines |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation |
| 1.13.11.49 | chlorite O2-lyase |
environmental protection |
bacteria with Cld play significant roles in the bioremediation of industrially contaminated sites and also in wastewater treatment |
| 2.7.4.1 | ATP-polyphosphate phosphotransferase |
environmental protection |
bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in Escherichia coli. Specific application of this process to polyphosphate is of potential application for biological phosphate removal |
| 2.8.3.16 | formyl-CoA transferase |
environmental protection |
bacterial oxalate-degrading function, microbiological processes are considered as the main oxalate sinks in natural environments, in soil oxalate from fungi, plant root exudates and decaying plant tissues display powerful metal chelating properties. Oxalate takes part in plant nutrition status by increasing the availability of phosphate and other poorly soluble micro-nutriments, through its ability to complex and remove excess metal cations. It also plays an important role in the detoxification of heavy metals in the vicinity of plant roots. |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
because the halogenated substrates are often environmentally toxic industrial byproducts, the enzyme has been suggested to be an useful catalyst for biodegradation and bioremediation |
| 1.14.13.50 | pentachlorophenol monooxygenase |
environmental protection |
bioaugmentation of groundwater with known Sphingobium chlorophenolicum L-1, amendment of nutrients, and air sparging result in an enhanced degradation of pentachlorophenol and hence bioremediation of PCP-contaminated groundwater. The amendments to the site undergoing air sparging may result in more effective and less time-consuming bioremediation of pentachlorophenol-contaminated groundwater without adding significantly high cost and labor |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
bioconversion of plastics |
| 3.8.1.8 | atrazine chlorohydrolase |
environmental protection |
biodegradation by cells encapsulated in silica gel is an economical and environmentally friendly method for the removal of toxic chemicals from the environment. Recombinant Escherichia coli expressing atrazine chlorohydrolase are encapsulated in organically modified silica gels composed of TEOS, silica nanoparticles, and either phenyltriethoxysilane or methyltriethoxysilane. The optimized PTES and MTES gels have atrazine biodegradation rates of 0.041 and 0.047 mol/ml gel, respectively. The rates are approximately 80% higher than that measured in the TEOS gel. Optimized hydrophobic gel material design can be used to enhance both removal and biodegradation of hydrophobic chemicals like atrazine |
| 1.13.11.50 | acetylacetone-cleaving enzyme |
environmental protection |
biodegradation by the enzyme of the widely used industrial chemical acetylacetone, i.e. 2,4-pentanedione, which has toxic effects, in a membrane bioreactor, determination of operational stability of the enzyme in the reactor at different temperatures, simulations |
| 1.11.1.7 | peroxidase |
environmental protection |
biodegradation of toxic and carcinogenic phenolic contaminants and related compounds in industrial effluents. Calotropis procera is a drought-resistant local plant that grows wild in the natural habitat of Nigerian throughout the year. Calotropis procera root could be an environmentally sustainable source of peroxidase for a low technological solution for phenol remediation |
| 3.8.1.8 | atrazine chlorohydrolase |
environmental protection |
bioremidiation, use of enhanced expression of a modified bacterial atrazine chlorohydrolase, p-AtzA, in transgenic grasses, tall fescue or Festuca arundinacea, ryegrass or Lolium perenne, and switchgrass or Panicum virgatum, and the legume alfalfa, Medicago sativa, for the biodegradation of atrazine |
| 4.2.2.2 | pectate lyase |
environmental protection |
biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process |
| 2.1.1.201 | 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase |
environmental protection |
BoCOQ5-2 methyltransferase is a facilitator of selenium volatilization, biologically based selenium volatilization is a particular area of interest for its potential in making detoxification of selenium pollution highly effective |
| 1.3.3.5 | bilirubin oxidase |
environmental protection |
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes |
| 1.13.11.2 | catechol 2,3-dioxygenase |
environmental protection |
C23O appears to be very powerful and useful tools in the biotreatment of wastewaters and soil decontamination |
| 3.5.5.7 | Aliphatic nitrilase |
environmental protection |
Candida guilliermondii UFMG-Y65 might be useful for the bioremediation of environments contaminated with nitriles |
| 4.2.1.1 | carbonic anhydrase |
environmental protection |
carbon dioxide absorption into carbonate solutions, promoted by the enzyme carbonic anhydrase, is proposed as potential technology for CO2 capture. The use of solid CA-based biocat-alysts allows the enzyme recovery and reuse under continuous operating conditions typical of industrial applications |
| 3.2.1.4 | cellulase |
environmental protection |
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose |
| 3.2.1.14 | chitinase |
environmental protection |
chitin and chitinolytic bacteria addition can reduce the population of fungal plant pathogens in soil and enhance the growth of plants. In this biocontrol and environmental bioremediation, communities of soil bacteria and the addition of chitinous materials play an important role |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
chloroperoxidase shows oxidative dehalogenation activity and is significantly more robust than other peroxidases and functions under harsher reaction conditions compared to other biocatalysts. Expanding the scope of reactivity achieved by the enzyme may be beneficial for industrial and biotechnological functions in the future. This considerable extension of already known activities could lead to the use of the enzyme as a biocatalyst in the field of bioremediation and a broader understanding of both how peroxidases and cytochrome P450s react with halogenated organic substrates |
| 3.5.1.4 | amidase |
environmental protection |
convenient treatment of acetonitrile-containing wastes using the tandem combination of nitrile hydratase (Rhodococcus pyridinivorans S85-2) and amidase-producing microorganisms (Brevundimonas diminuta AM10-C-1) |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters |
| 1.11.1.18 | bromide peroxidase |
environmental protection |
CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters |
| 1.15.1.1 | superoxide dismutase |
environmental protection |
Cu/Zn superoxide dismutase might be used as a bioindicator of the aquatic environmental pollution and cellular stress in pearl oyster |
| 4.2.1.104 | cyanase |
environmental protection |
cyanate and its derivatives are considered as environmental hazardous materials. Cyanate is released to the environment through many chemical industries and mining wastewater. Cyanase enzyme converts cyanate into CO2 and NH3 in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification. But such cyanate biodegradation system is probably insufficient due to the excess cyanate concentrations at contaminated sites. Evaluation of transgenic plant resistance to cyanate stress. The enzyme is a candidate for developing novel ecofriendly phytoremediation systems for cyanate detoxification |
| 1.10.3.2 | laccase |
environmental protection |
cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment |
| 3.5.2.15 | cyanuric acid amidohydrolase |
environmental protection |
cyanuric acid hydrolases are of industrial importance because of their use in aquatic recreational facilities to remove cyanuric acid, a stabilizer for the chlorine. Degradation of excess cyanuric acid is necessary to maintain chlorine disinfection in the waters |
| 1.10.3.2 | laccase |
environmental protection |
decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters |
| 1.10.3.2 | laccase |
environmental protection |
decolorization of industrial dyes. Evans blue decolorization and detoxification |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
decolorization of textile dyes |
| 3.1.1.3 | triacylglycerol lipase |
environmental protection |
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids |
| 4.2.1.84 | nitrile hydratase |
environmental protection |
degradation of nitrile waste |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
degradation of recalcitrant pollutants |
| 1.10.3.2 | laccase |
environmental protection |
degradation of synthetic dyes from wastewater using biological treatment |
| 1.10.3.2 | laccase |
environmental protection |
deinking of old newspaper, indigo carmine decolorization |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
environmental protection |
detoxification of halogenated herbicides, solvents and other xenobiotic compounds by immobilized enzyme |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
detoxification of mercury by immobilized mercuric reductase |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
environmental protection |
detoxification of nerve agent exposed environments |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
detoxification of organomercury compounds is of critical importance. The bioorganometallic chemistry of mercury in a sulfur-rich coordination environment is studied in order emulate the structure and function of MerB. One of the three non-structural cysteine residues of MerB that are crucial for enzymatic activity is required to coordinate [HgR]+ in a linear manner, a second cysteine is required to activate the Hg-alkyl group toward protolytic cleavage, and the third cysteine is required to effect the cleavage reaction. |
| 1.14.13.50 | pentachlorophenol monooxygenase |
environmental protection |
development of biological methods for the decontamination of halophenol-polluted sites |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
DhaA displayed on the surface of Bacillus subtilis spores retains enzymatic activity, which suggests that it can be used effectively in applications including bioremediation of contaminated environments |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
DhaA is capable of degrading 1,2,3-trichloropropane, TCP, an industrial waste product that is toxic, extremely recalcitrant to biodegradation, and expensive to dispose of by physical or chemical methods |
| 3.5.2.15 | cyanuric acid amidohydrolase |
environmental protection |
di- and trichloroisocyanuric acids are widely used as water disinfection agents, but cyanuric acid accumulates with repeated additions and must be removed to maintain free hypochlorite for disinfection. The study describes the development of methods for using a cyanuric acid-degrading enzyme contained within nonliving cells that are encapsulated within a porous silica matrix |
| 3.5.2.15 | cyanuric acid amidohydrolase |
environmental protection |
di- and trichloroisocyanuric acids are widely used as water disinfection agents, but cyanuric acid accumulates with repeated additions and must be removed to maintain free hypochlorite for disinfection. The study describes the development of methods for using a cyanuric acid-degrading enzyme contained within nonliving cells that are encapsulated within a porous silica matrix. The optimum enzyme for these purposes was found to be the cyanuric acid hydrolase from Moorella thermoacetica. A water-recycling, flowthrough system is constructed and shown to be effective in removing 10 mM M cyanuric acid, a concentration well above that encountered in real-world disinfection processes |
| 1.1.1.149 | 20alpha-hydroxysteroid dehydrogenase |
environmental protection |
diesel exhaust components are inhibitory on 20alpha-hydroxysteroid dehydrogenase in liver and lung cytosol, with little inhibition in kidney cytosol |
| 2.7.4.1 | ATP-polyphosphate phosphotransferase |
environmental protection |
E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater |
| 4.1.99.11 | benzylsuccinate synthase |
environmental protection |
enzyme BSS and the growing number of additional fumarate-adding enzymes have become model cases for environmental processes in contaminated soils and deep anoxic subsediment habitats, and their isotopic preferences and conserved sequences serving as templates for molecular probes are employed as tools for monitoring these processes in situ |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
enzyme DadB and its host, Alcanivorax dieselolei strain B-5, are of potential use for biocatalysis and bioremediation applications |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
environmental protection |
enzyme DFPase can be used as in vivo detoxifying agent for elimination of organophosphorus chemicals, used as pesticides and warfare nerve agent, e.g. sarin, soman, or tabun |
| 4.4.1.11 | methionine gamma-lyase |
environmental protection |
enzyme is not an important source of volatile methanethiol |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
enzyme MerA is a promising candidate for Hg2+ bioremediation |
| 1.12.2.1 | cytochrome-c3 hydrogenase |
environmental protection |
enzyme might be useful in development of a mechanism to remove contaminating uranium from groundwaters |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
enzyme might be utilized for bioremediation of organohalide-contaminated industrial waste |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
enzymes showing phosphotriesterase activity are capable of hydrolysing organophosphate phosphotriesters, a class of synthetic compounds employed worldwide both as insecticides and chemical warfare agents. Thermostable enzymes able to hydrolyse organophosphate phosphotriesters are considered good candidates for the set-up of efficient detoxification tools |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
enzymes showing phosphotriesterase activity are capable of hydrolysing the organophosphate phosphotriesters, a class of synthetic compounds employed worldwide both as insecticides and chemical warfare agents. Thermostable enzymes able to hydrolyse organophosphate phosphotriesters are considered good candidates for the set-up of efficient detoxification tools |
| 1.8.5.5 | thiosulfate reductase (quinone) |
environmental protection |
Escherichia coli expressing thiosulfate reductase genes (phsABC) from Salmonella typhimurium is able to remove significant amounts of heavy metals from the medium within 24 h: 99% of zinc up to 500 microM, 99% of lead up to 200 microM, 99% of 100 icroM and 91% of 200 icroM cadmium. In a mixture of 100 microM each of cadmium, lead, and zinc, the strain removes 99% of the total metals from solution within 10 h. Cadmium is removed first, lead second, and zinc last |
| 1.8.5.5 | thiosulfate reductase (quinone) |
environmental protection |
Escherichia coli strains harboring thiosulfate reductase gene phsABC expression constructs show higher thiosulfate reductase activity and produce significantly more sulfide than the control strains under both aerobic and anaerobic conditions. The most effecitve expression construct produces thiosulfate reductase at the highest level and removes the most cadmium from solution under anaerobic conditions: 98% of all concentrations up to 150 microM and 91% of 200 microM. The metal removed from solution precipitates as a complex of cadmium and sulfur, most likely cadmium sulfide |
| 2.8.4.1 | coenzyme-B sulfoethylthiotransferase |
environmental protection |
expression of methyl-coenzyme M reductase from an unculturable organism in Methanosarcina acetivorans to effectively run methanogenesis in reverse. Methanosarcina acetivorans cells heterologously producing methyl-coenzyme M reductase consume up to 9% of methane (corresponding to 109 micromol of methane) after 6 weeks of anaerobic growth on methane and utilize 10 mM FeCl3 as an electron acceptor. When incubated on methane for 5 days, high-densities of cells consume 15% methane (corresponding to 143 micromol of methane), and produce 10.3 mM acetate (corresponding to 52 micromol of acetate) |
| 1.10.3.2 | laccase |
environmental protection |
fast biodegradation of 2,4-dichlorophenol, a potent xenobiotic compound |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater |
| 4.1.2.43 | 3-hexulose-6-phosphate synthase |
environmental protection |
formaldehyde is thought to be the cause of sick house syndrome, transgenic plants harboring the ribulose monophosphate pathway could be useful to improve air pollution in the indoor environment |
| 1.3.1.32 | maleylacetate reductase |
environmental protection |
further evolution to more catalytically active PcpE may be an important contributor to improved Sphingobium chlorophenolicum L-1-mediated bioremediation of pentachlorophenol |
| 1.14.99.39 | ammonia monooxygenase |
environmental protection |
gene amoA, which encodes the key subunit of the AMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment |
| 1.14.18.3 | methane monooxygenase (particulate) |
environmental protection |
gene pmoA, which encodes the key subunit of the pMMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
generation of a coupled enzyme system constructed with azoreductase and glucose 1-dehydrogenase for removal of methyl red, evaluation, overview |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
Geobacter sulfurreducens useful for the decontamination of environments polluted with azo dyes. The contribution of extracellular respiration to pollutants reduction will broaden the environmental applications |
| 1.10.3.2 | laccase |
environmental protection |
good application prospect in wastewater treatment and dye degradation. error-prone PCR is a feasible method to improve the degradation activity of laccase for environmental pollutants, which provide a basis for the application of laccase on dye degradation and other environmental pollutants |
| 2.5.1.47 | cysteine synthase |
environmental protection |
H2S is a major environmental pollutant, highly toxic to living organisms at high concentrations. Even at low concentrations, it causes an unpleasant odor from wetlands, especially from wastewater. Plants can utilize hydrogen sulfide as a sulfur source to synthesize cysteine. It is thus feasible to use aquatic plants, which possess high potential for sulfur assimilation, to remove hydrogen sulfide from the wetland. Transgenic rice plants over-expressing cysteine synthase exhibit 3fold elevated cysteine synthase activity, and incorporate more H2S into cysteine and glutathione than their wild type counterparts upon exposure to a high level of H2S. Overexpression of cysteine synthase in aquatic plants is a viable approach to remove H2S from polluted environments |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
haloalkane dehalogenases are exploited for clean-up of groundwater contaminated by halogenated compounds, removal of the side-products from chemical synthesis, and biosensors detecting halogenated contaminants in the environment |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants |
| 1.7.1.2 | Nitrate reductase [NAD(P)H] |
environmental protection |
hexahydro-1,3,5-trinitro-1,3,5-triazine is widely used for military and commercial purposes due to its high explosive properties. Hexahydro-1,3,5-trinitro-1,3,5-triazine and its degradation products are toxic, mutagenic and carcinogenic to humans and other biological systems. The biotransformation of hexahydro-1,3,5-trinitro-1,3,5-triazine by NAD(P)H nitrate reductase from Aspergillus niger under anaerobic conditions |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
HLD-containing bacteria are interesting as a cleanup technology for toxic haloalkane wastes produced from industries such as plastics and pesticides manufacture |
| 1.14.99.39 | ammonia monooxygenase |
environmental protection |
identification of organic oxidation products and comparison of the reactivities of monohalogenated ethanes and n-chlorinated C1 to C4 alkanes for oxidation by whole cells of Nitrosomonas europaea. The dehalogenating potential of the ammonia monooxygenase in Nitrosomonas europaea may have practical applications for the detoxification of contaminated soil and groundwater |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
environmental protection |
immobilized enzyme exhibits great potential for application in bioremediation |
| 1.20.9.1 | arsenate reductase (azurin) |
environmental protection |
important implications for biomediation of arsenite contaminated soils and groud water |
| 4.2.1.24 | porphobilinogen synthase |
environmental protection |
in free-living bird species, a decrease is observed in ALAD activity in Griffon vultures and Eagle owls exposed to Pb. Negative relationships are found between ALAD ratio or ALAD activity and logarithmic blood Pb levels in Griffon vultures and Eagle owls, and these relationships are stronger in areas with the highest Pb exposure. ALAD activity in Slender-billed gull and Audouin's gull species may be considerably normal, since very low blood Pb concentrations and no correlations are found |
| 1.13.11.1 | catechol 1,2-dioxygenase |
environmental protection |
in gasoline contaminated environments, aromatic hydrocarbon degrading Rhodococcus populations can be identified based upon the detection and sequence analysis of catechol 1,2-dioxygenase gene. Rhodococcus species are important members of the bacterial community involved in the degradation of aromatic contaminants and their specific detection can help assess functions and activities in the contaminated environments |
| 4.2.3.27 | isoprene synthase |
environmental protection |
isoprene emission patterns in transgenic tobacco plants are remarkably similar to naturally emitting plants under a wide variety of conditions. Emissions correlate with photosynthetic rates in developing and mature leaves, and with the amount of isoprene synthase protein in mature leaves. Isoprene synthase protein levels do not change under short-term increase in heat/light, despite an increase in emissions under these conditions. A robust circadian pattern can be observed in emissions from long-day plants. Substrate supply and changes in enzyme kinetics rather than changes in isoprene synthase levels or post-translational regulation of activity seem to be the primary controls on isoprene emission in mature transgenic tobacco leaves |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins |
| 1.10.3.2 | laccase |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment |
| 1.10.3.2 | laccase |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without addition of an expensive redox mediator |
