EC Number   |
Title |
Organism |
|---|
    4.99.1.2 | Mechanistic pathways of mercury removal from the organomercurial lyase active site |
Escherichia coli |
| 4.99.1.2 | Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB insight into the key role of the active site aspartic acid in Hg-carbon bond cleavage and metal binding specificity |
Escherichia coli |
| 4.99.1.2 | Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB insight into the key role of the active site aspartic acid in Hg-carbon bond cleavage and metal binding specificity |
Priestia megaterium |
| 4.99.1.2 | Structural and biochemical characterization of organotin and organolead compounds binding to the organomercurial lyase MerB provide new insights into its mechanism of carbon-metal bond cleavage |
Escherichia coli |
| 4.99.1.2 | A PMA degrading constitutive organomercurial lyase in a broad-spectrum mercury resistant Bacillus pasteurii strain DR2 |
Sporosarcina pasteurii |
| 4.99.1.2 | A stable mercury-containing complex of the organomercurial lyase MerB: catalysis, product release, and direct transfer to MerA |
Escherichia coli |
| 4.99.1.2 | Bacterial mer operon-mediated detoxification of mercurial compounds: a short review |
Staphylococcus aureus |
| 4.99.1.2 | Bacterial organomercurial lyase: Mechanistic studies on a protonolytic organomercurial cleaving enzyme in mercurial detoxification |
Escherichia coli |
| 4.99.1.2 | Bacterial organomercurial lyase: Mechanistic studies on a protonolytic organomercurial cleaving enzyme in mercurial detoxification |
Escherichia coli overproducing |
| 4.99.1.2 | Bacterial organomercurial lyase: Novel enzymatic protonolysis of organostannanes |
Escherichia coli |
