4.99.1.2: alkylmercury lyase
This is an abbreviated version!
For detailed information about alkylmercury lyase, go to the full flat file.
Word Map on EC 4.99.1.2
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4.99.1.2
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methylmercury
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mercury-resistant
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protonolysis
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phytoremediation
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phenylmercury
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hg-resistant
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environmental protection
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biomagnifies
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mercury-contaminated
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biotechnology
- 4.99.1.2
- methylmercury
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mercury-resistant
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protonolysis
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phytoremediation
- phenylmercury
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hg-resistant
- environmental protection
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biomagnifies
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mercury-contaminated
- biotechnology
Reaction
Synonyms
alkylmercury mercuric-lyase, lyase, alkylmercury, merB, MerB1, MerB2, MerB3, organomercurial lyase, organomercury lyase
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General Information
General Information on EC 4.99.1.2 - alkylmercury lyase
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metabolism
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key enzyme for the detoxification and bioremediation of the organomercurial compound
physiological function
additional information
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organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
physiological function
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organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
physiological function
organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
physiological function
organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
physiological function
-
organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
-
physiological function
-
organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
-
physiological function
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organomercury lyase is a key enzyme in bacterial detoxification and bioremediation of organomercurials
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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.
additional information
theoretical insights into the mechanism of Hg-C bond protonolysis in methyl mercury coordinated by the tris(2-mercapto-1-tert-butylimidazolyl)hydroborato ligand, the structural and functional analogue of the organomercurial lyase MerB, different cleavage pathways including both frontside and backside attack transition states are systematically studied by the hybrid density functional method B3LYP