Bacterial organomercurial lyase: overproduction, isolation, and characterization

Biochemistry. 1986 Nov 4;25(22):7186-92. doi: 10.1021/bi00370a063.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lyases / genetics
  • Lyases / isolation & purification
  • Lyases / metabolism*
  • Organomercury Compounds / metabolism
  • Plasmids
  • Substrate Specificity


  • Organomercury Compounds
  • Lyases
  • alkylmercury lyase