Application | Comment | Organism |
---|---|---|
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. | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli R831b | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
RHg+ + H+ | - |
Escherichia coli | RH + Hg2+ | - |
? | |
RHg+ + H+ | - |
Escherichia coli R831b | RH + Hg2+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alkylmercury mercuric-lyase | - |
Escherichia coli |
merB | - |
Escherichia coli |
organomercurial lyase | - |
Escherichia coli |