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Literature summary extracted from

  • Wahba, H.M.; Lecoq, L.; Stevenson, M.; Mansour, A.; Cappadocia, L.; Lafrance-Vanasse, J.; Wilkinson, K.J.; Sygusch, J.; Wilcox, D.E.; Omichinski, J.G.
    Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB insight into the key role of the active site aspartic acid in Hg-carbon bond cleavage and metal binding specificity (2016), Biochemistry, 55, 1070-1081 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.99.1.2 expression in Escherichia coli Priestia megaterium
4.99.1.2 expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.99.1.2 mutant D99S, in complex with Cu(II), Hg and p-chloromercuribenzoate, to 1.24-1.95 A resolution Escherichia coli
4.99.1.2 to 1.24 A resolution, comparison with strucutre of Escherichia coli MerB mutant D99S Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
4.99.1.2 D99N Cu(II) is bound to the active site cysteine residues Escherichia coli
4.99.1.2 D99S mutation mimicks the sequence of Bacillus megaterium MerB. Cu(II) is bound to the active site cysteine residues and is displaced following the addition of either an organomercurial substrate or an ionic mercury product Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.99.1.2 copper paramagnetic Cu(II) is bound to the active site cysteine residues of mutant MerB D99S Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.99.1.2 Escherichia coli P77072
-
-
4.99.1.2 Priestia megaterium Q7DJN2 isoform MerB2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.99.1.2
-
 Priestia megaterium
4.99.1.2 enzyme copurifies with bound Cu2+ Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.99.1.2 merB
-
 Escherichia coli
4.99.1.2 MerB2
-
 Priestia megaterium