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