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

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.

authors

• Begley, Tadhg

published proceedings

• Biochemistry

altmetric score

• 6

author list (cited authors)

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

citation count

• 73

complete list of authors

• Begley, TP||Walts, AE||Walsh, CT

publication date

• November 1986

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

• Amino Acid Sequence
• Escherichia Coli
• Hydrogen-Ion Concentration
• Kinetics
• Lyases
• Organomercury Compounds
• Plasmids
• Substrate Specificity

PubMed Central ID

• 3542021

Digital Object Identifier (DOI)

• 10.1021/bi00370a063

start page

• 7186

end page

• 7192

volume

• 25

issue

• 22

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fbi00370a063