EC Number   |
Recommended Name |
Application  |
|---|
    4.2.1.84 | nitrile hydratase |
environmental protection |
degradation of nitrile waste |
| 4.2.1.84 | nitrile hydratase |
environmental protection |
NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste |
| 4.2.1.104 | cyanase |
environmental protection |
potential biotechnological application in environmental detoxification |
| 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 |
| 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 |
| 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 |
| 4.2.2.2 | pectate lyase |
environmental protection |
the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption |
| 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 |
| 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 |
| 4.2.3.27 | isoprene synthase |
environmental protection |
regulation of isoprene emission. Upon darkening a leaf, isoprene emission falls nearly to zero but then increases for several min before falling back to nearly zero. Time of appearance of this burst of isoprene is highly temperature dependent, occurring sooner at higher temperatures. During a rapid temperature switch from 30°C to 40°C, isoprene emission increases transiently with concomitant increase in isoprene synthase activity, while dimethylallyl diphosphate level stays constant during the switch. One h after switching to 40!, the amount of dimethylallyl diphosphate falls but the rate constant for isoprene synthase remains constant, indicating that the high temperature falloff in isoprene emission results from a reduction in the supply of dimethylallyl diphosphate rather than from changes in isoprene synthase activity |
| 4.4.1.11 | methionine gamma-lyase |
environmental protection |
enzyme is not an important source of volatile methanethiol |
| 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. |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
transgenic merB plants express high levels of MerB protein and show some evidence of higher resistance to the organic mercury than wild-type plants, in order to be useful in eastern cottonwood trees to degrade methylmercury at mercury contaminated aquatic sites, merB should be combined with other genes such as merA |
| 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. |
| 7.2.2.2 | ABC-type Cd2+ transporter |
environmental protection |
overexpression of this fungal transporter in plants can be useful for phytoremediation of lead and cadmium polluted soils |
