Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.99.1.2 extracted from

  • Wahba, H.M.; Stevenson, M.J.; Mansour, A.; Sygusch, J.; Wilcox, D.E.; Omichinski, J.G.
    Structural and biochemical characterization of organotin and organolead compounds binding to the organomercurial lyase MerB provide new insights into its mechanism of carbon-metal bond cleavage (2017), J. Am. Chem. Soc., 139, 910-921 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.99.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with dimethyltin, diethyltin, and triethyltin, to 1.53-2.0 A resolution Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
dimethyltin initial binding is to residue D99, and compound subsequently binds to C96, which induces a conformation change in the active site Escherichia coli
trimethyllead compound is not cleaved and binds only to residue D99 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77072
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diethyllead + H+
-
 Escherichia coli 2 ethane + Pb2+
-
 ?
diethyltin + 2 H+
-
 Escherichia coli 2 ethane + Sn2+
-
 ?
additional information MerB cleavage reaction involves heterolytic carbon-metal bond cleavage, Cys thiol deprotonation, protonation of the formal carbanion, and metal binding to the Cys thiolate. The first two steps are endothermic, and the last two would be exothermic Escherichia coli ?
-
 ?