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Literature summary for 4.99.1.2 extracted from

  • Lafrance-Vanasse, J.; Lefebvre, M.; Di Lello, P.; Sygusch, J.; Omichinski, J.G.
    Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation (2009), J. Biol. Chem., 284, 938-944.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and mutant MerBs. MerB, C96S MerB, C159S MerB, and C160S MerB, in the free and mercury-bound form, by vapor diffusion at 23°C and pH 5.5 using either a 1:1 or 1:2 mixture of protein solution, containing 8 mg/ml initial protein concentration, and precipitant buffer, respectively, that is equilibrated against a reservoir of precipitant buffer , X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
C159S site-directed mutagenesis, inactive mutant Escherichia coli
C160S site-directed mutagenesis, mutant enzyme with moderately reduced activity Escherichia coli
C96S site-directed mutagenesis, inactive mutant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77072 gene merB encoded on plasmid R831b
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mechanism for the cleavage of the carbon-mercury bond and the formation of the MerB-Hg complex, modelling, overview. Hg2+ binding structure of wild-type and mutant enzymes, overview Escherichia coli ?
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Synonyms

Synonyms Comment Organism
merB
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Escherichia coli