Literature summary extracted from

Parks, J.M.; Guo, H.; Momany, C.; Liang, L.; Miller, S.M.; Summers, A.O.; Smith, J.C.
Mechanism of Hg-C protonolysis in the organomercurial lyase MerB (2009), J. Am. Chem. Soc., 131, 13278-13285.

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.99.1.2	Escherichia coli	P77072	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.99.1.2	RHg+ + H+	-	Escherichia coli	RH + Hg2+	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
4.99.1.2	merB	-	Escherichia coli
4.99.1.2	organomercurial lyase	-	Escherichia coli

General Information

EC Number	General Information	Comment	Organism
4.99.1.2	additional information	quantum chemical calculations have been performed to compare the two chief candidate mechanisms for the Hg-C protonolysis catalyzed by the organomercurial lyase, MerB. The coordination of R-Hg(II) by two cysteine thiolates is necessary and sufficient to activate the Hg-C bond toward protonolysis.	Escherichia coli

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Release 2023.1 (January 2023)