Bacterial organomercurial lyase: overproduction, isolation, and characterization. Academic Article uri icon

abstract

  • 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.

altmetric score

  • 6

author list (cited authors)

  • Begley, T. P., Walts, A. E., & Walsh, C. T.

citation count

  • 66

publication date

  • November 1986