EC Number   |
Application |
Reference |
|---|
    4.99.1.2 | biotechnology |
coexpression of enzyme and mercuric reductase in Arabidopsis thaliana leads to growth on 50fold higher methylmercury concentrations than wild-type plants |
653291 |
| 4.99.1.2 | biotechnology |
engineering of enzyme as to be targeted for accumulation in the endoplasmic reticulum and for secretion to the cell wall rendering the expressing plants resistant to organic mercury |
653539 |
| 4.99.1.2 | 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 |
701887 |
| 4.99.1.2 | 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. |
705415 |
| 4.99.1.2 | 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. |
-, 682859 |
| 4.99.1.2 | 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 |
680110 |
