Bacterial organomercurial lyase: overproduction, isolation, and characterization.
Organomercurial lyase mediates the first of two steps in the microbial detoxification of organomercurial salts. This enzyme encoded on the plasmid R831 obtained from Escherichia coli J53-1 has been overproduced to the level of 3% of the soluble cell protein in E. coli by a construction using the T7 promoter. The enzyme has been purified to homogeneity in quantity in three steps. It is a monomer of Mr 22,400 with no detectable cofactors or metal ions. It catalyzes the protonolysis of the C-Hg bond in a wide range of organomercurial salts (primary, secondary, tertiary, alkyl, vinyl, allyl, and aryl) to the hydrocarbon and mercuric ion with turnover rates in the range of 1-240 min-1.
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008190:Lyases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D009941:Organomercury Compounds / Q000378:metabolism; D010957:Plasmids; D013379:Substrate Specificity
D009941:Organomercury Compounds; D008190:Lyases; C050953:alkylmercury lyase