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Information on EC 4.99.1.2 - alkylmercury lyase
for references in articles please use BRENDA:EC4.99.1.2
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EC Tree 4 Lyases
4.99 Other lyases
4.99.1 Sole sub-subclass for lyases that do not belong in the other subclasses
4.99.1.2 alkylmercury lyase
IUBMB Comments
Acts on CH3Hg+ and a number of other alkylmercury compounds, in the presence of cysteine or other thiols, liberating mercury as a mercaptide.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 4.99.1.2
- methylmercury
-
mercury-resistant
-
protonolysis
-
phytoremediation
- phenylmercury
-
hg-resistant
- environmental protection
-
biomagnifies
-
mercury-contaminated
- biotechnology
showSynonyms
organomercurial lyase, merb3, organomercury lyase, merb1, merb2, alkylmercury lyase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkylmercury mercuric-lyase
lyase, alkylmercury
-
-
-
-
merB
MerB1
MerB2
MerB3
organomercurial lyase
organomercury lyase
organomercurial lyase
-
-
-
-
organomercury lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an alkylmercury + H+ = an alkane + Hg2+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phenylmercury acetate degradation
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SYSTEMATIC NAME
IUBMB Comments
alkylmercury mercuric-lyase (alkane-forming)
Acts on CH3Hg+ and a number of other alkylmercury compounds, in the presence of cysteine or other thiols, liberating mercury as a mercaptide.
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CAS REGISTRY NUMBER
COMMENTARY
72560-99-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ethylmercury chloride
?
Substrates: merB3 gene product
Products: -
Products: -
?
fluorescein mercury acetate
?
Substrates: merB3 gene product
Products: -
Products: -
?
methylmercury chloride
?
Substrates: merB3 gene product
Products: -
Products: -
?
organo-tin compounds
?
-
Substrates: degradation of biocides, resistant organisms
Products: -
Products: -
?
organomercurial salts + H+
?
-
Substrates: primary, secondary, tertiary, alkyl, vinyl, allyl, aryl
Products: -
Products: -
?
p-hydroxymercuribenzoate + H+
Hg2+ + p-hydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
vinyl mercuric bromide + H+
ethene + Hg+ + Br-
-
Substrates: -
Products: -
Products: -
?
alkyl mercuric halides + H+
?
-
Substrates: primary, secondary, tertiary
Products: -
Products: -
?
alkyl mercuric halides + H+
?
-
Substrates: primary, secondary, tertiary
Products: -
Products: -
?
CH3Hg+ + H+
CH4 + Hg2+
Substrates: 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
Products: -
Products: -
?
CH3Hg+ + H+
Hg2+ + CH4
Substrates: the growth rates of both the wild-type and ppk/merTtransgenic tobacco callus are largely inhibited by CH3Hg+ in a dose-dependent manner
Products: -
Products: -
?
crotonyl mercuric bromide + H+
crotonaldehyde + Hg2+ + Br-
-
Substrates: -
Products: -
Products: -
?
crotonyl mercuric bromide + H+
crotonaldehyde + Hg2+ + Br-
-
Substrates: -
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
Substrates: about 12% organomercury remaining after 24 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
-
Substrates: about 1% organomercury remaining after 72 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
-
Substrates: about 13% organomercury remaining after 24 h incubation
Products: -
Products: -
?
ethylmercury chloride
Hg2+ + ?
-
Substrates: about 13% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methyl mercuric chloride + H+
CH4 + Hg2+ + Cl-
-
Substrates: -
Products: -
Products: -
?
methyl mercuric chloride + H+
CH4 + Hg2+ + Cl-
-
Substrates: -
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
Substrates: best substrate, about 5% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
Substrates: about 12% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
Substrates: best substrate, about 5% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
-
Substrates: best substrate, less than 1% organomercury remaining after 72 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
-
Substrates: about 52% organomercury remaining after 24 h incubation
Products: -
Products: -
?
methylmercury chloride
Hg2+ + ?
-
Substrates: about 52% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
Substrates: merB3 gene product
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
Substrates: about 7% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
Substrates: about 12% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
Substrates: about 7% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
Substrates: about 40% organomercury remaining after 72 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
Substrates: about 18% organomercury remaining after 24 h incubation
Products: -
Products: -
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
Substrates: about 18% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenyl mercuric acetate + H+
benzene + Hg2+ + acetate
Substrates: -
Products: -
Products: -
?
phenyl mercuric acetate + H+
benzene + Hg2+ + acetate
-
Substrates: -
Products: -
Products: -
?
phenylmercuric acetate + H+
benzene + Hg+ + Cl-
-
Substrates: -
Products: -
Products: -
?
phenylmercuric acetate + H+
benzene + Hg+ + Cl-
-
Substrates: -
Products: -
Products: -
?
phenylmercury acetate
?
Substrates: about 45% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
Substrates: about 45% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
Substrates: merB3 gene product
Products: -
Products: -
?
phenylmercury acetate
?
Substrates: about 50% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
Substrates: about 65% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
Substrates: about 50% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
-
Substrates: about 65% organomercury remaining after 72 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
-
Substrates: about 55% organomercury remaining after 24 h incubation
Products: -
Products: -
?
phenylmercury acetate
?
-
Substrates: about 55% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
Substrates: about 10% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
Substrates: about 7% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
Substrates: about 12% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
Substrates: about 7% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
-
Substrates: about 3% organomercury remaining after 72 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
-
Substrates: about 13% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal
Hg2+ + ?
-
Substrates: about 13% organomercury remaining after 24 h incubation
Products: -
Products: -
?
thimerosal + H+
?
-
Substrates: i.e. sodium ethylmercurithiosalicylate
Products: -
Products: -
?
thimerosal + H+
?
-
Substrates: i.e. sodium ethylmercurithiosalicylate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: quantum chemical computations of the reaction steps leading to the removal of Hg2+ from MerB. The most straightforward pathway proceeds through proton transfer from the attacking thiol to Cys159, leading to its removal from the mercury coordination sphere, followed by a slower attack of a second thiol, which removes Cys96. The other pathway involves Asp99 in an accessory role and affords a lower activation enthalpy, around 14 kcal/mol. Kinetic simulation strongly suggests that in vivo the thiolate-only pathway is operative, and the Asp-assisted pathway is prevented by steric factors
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: dimethyl mercury
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CH3Hg+ + H+
CH4 + Hg2+
Substrates: 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
Products: -
Products: -
?
organo-tin compounds
?
-
Substrates: degradation of biocides, resistant organisms
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
paramagnetic Cu(II) is bound to the active site cysteine residues of mutant MerB D99S
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CH3Hg+
the growth rates of both the wild-type and ppk/merT-transgenic tobacco callus are largely inhibited by CH3Hg+ in a dose-dependent manner
dimethyltin
initial binding is to residue D99, and compound subsequently binds to C96, which induces a conformation change in the active site
dithiothreitol
-
50% inhibition at 0.0034 mM against 20 mM glutathion and at 0.019 mM against 20 mM cysteine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11 - 0.37
p-hydroxymercuribenzoate
-
pH 8.0, in presence of glutathione
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isoenzyme pIAAD3 80% conversion of phenyl mercuric acetate into inorganic mercury within 1 h of incubation at 37°C
additional information
isoenzyme pIAAD3 80% conversion of phenyl mercuric acetate into inorganic mercury within 1 h of incubation at 37°C
additional information
isoenzyme pIAAD3 80% conversion of phenyl mercuric acetate into inorganic mercury within 1 h of incubation at 37°C
additional information
-
isoenzyme pIAAD3 80% conversion of phenyl mercuric acetate into inorganic mercury within 1 h of incubation at 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
The organomercurial lyase gene of plasmid pMR26 (GenBank/DDBJ accession no. D83080) is amplified by PCR using two specific primers. The pBMK01 plasmid is transformed into Agrobacterium tumefaciens LBA4404 by electroporation, and its sequence is confirmed. The ppk/merT-transgenic tobacco (T3) is then transformed with this Agrobacterium tumefaciens
TrEMBL
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
key enzyme for the detoxification and bioremediation of the organomercurial compound
physiological function
additional information
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
-
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
-
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
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.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22400
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MerB has a high structural similarity to the copper binding protein NosL, MerB and apo NosL are the only members of a new structural superfamily, each containing two perpendicularly arranged bbab motifs
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with dimethyltin, diethyltin, and triethyltin, to 1.53-2.0 A resolution
mutant D99S, in complex with Cu(II), Hg and p-chloromercuribenzoate, to 1.24-1.95 A resolution
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
to 1.24 A resolution, comparison with strucutre of Escherichia coli MerB mutant D99S
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C160S
site-directed mutagenesis, mutant enzyme with moderately reduced activity
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
additional information
additional information
-
engineering of enzyme as to be targeted for accumulation in the endoplasmic reticulum and for secretion to the cell wall rendering the expressing plants resistant to organic mercury
additional information
-
coexpression of enzyme and mercuric reductase in Arabidopsis thaliana leads to growth on 50fold higher methylmercury concentrations than wild type plants
additional information
The organomercurial lyase gene of plasmid pMR26 (GenBank/DDBJ accession no. D83080) is amplified by PCR using two specific primers. The pBMK01 plasmid is transformed into Agrobacterium tumefaciens LBA4404 by electroporation, and its sequence is confirmed. The ppk/merT-transgenic tobacco (T3) is then transformed with this Agrobacterium tumefaciens, the tobacco callus shows more resistance to CH3Hg+ and accumulated significantly more mercury from CH3Hg+-containing medium than does the ppk/merT-transgenic and wild-type tobaccos
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Agrobacterium tumefaciens are transfected with MerB, leaves of Populus deltoides are transfected with MerB by soaking in MerB transfected Agrobacterium tumefaciens bacteria, generation of transgenic merB Populus deltoides plants which are more resistant to organic mercury than wild-type plants in vitro, probably by converting it to Hg(II) in plant tissues
-
co-expression in Escherichia coli DH5alpha with the luciferase gene luxAB from Vibrio harveyi
expressed in Escherichia coli BL21 (DE3) pLysS cells
expression in Escherichia coli
gene merB, overexpression in Arabidopsis thaliana of cytoplasmic MerB allows the transgenic plants to grow at 5fold higher methyl mercury concentrations compared to wild-type controls, the additional expression of merApe9 in merA/merB hybrid plants further improves tolerance by a factor of 10 and promots efficient phenyl mercury removal and Hg0 volatization from a model solution, overexpression in Nicotiana tabacum chloroplasts, the phenotype shows doubled biomass yield with seedlings grown on medium with 0.4 mM phenyl-Hg2+. More than a 10fold higher volatization rate is further achieved by the targeting of MerB in the endoplasmic reticulum of merA/merB, where MerB exhibits more than 20times higher specific activity than in plants with cytoplasmically distributed MerB
-
gene pIAAD3, expression in Escherichia coli strains DH5ALPHA and SG13009
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
environmental protection
biotechnology
-
engineering of enzyme as to be targeted for accumulation in the endoplasmic reticulum and for secretion to the cell wall rendering the expressing plants resistant to organic mercury
biotechnology
-
coexpression of enzyme and mercuric reductase in Arabidopsis thaliana leads to growth on 50fold higher methylmercury concentrations than wild-type plants
environmental protection
-
transgenic merB plants express high levels of MerB protein and show some evidence of higher resistance to the organic mercury than wild-type plants, in order to be useful in eastern cottonwood trees to degrade methylmercury at mercury contaminated aquatic sites, merB should be combined with other genes such as merA
environmental protection
-
detoxification of organomercury compounds is of critical importance. The bioorganometallic chemistry of mercury in a sulfur-rich coordination environment is studied in order emulate the structure and function of MerB. One of the three non-structural cysteine residues of MerB that are crucial for enzymatic activity is required to coordinate [HgR]+ in a linear manner, a second cysteine is required to activate the Hg-alkyl group toward protolytic cleavage, and the third cysteine is required to effect the cleavage reaction.
environmental protection
a new transgenic tobacco plant for phytoremediation of CH3Hg+ pollution: The new ppk/merT/merB-transgenic tobacco plant, which contains the integrated bacterial merB gene encoding MerB, has the ability to tolerate and accumulate high levels of Hg2+ inside the plant cells from simulated soils, probably via a chelation mechanism of polyP with Hg2+, without releasing mercury vapor into the atmosphere
environmental protection
A recombinant whole-cell bacterial sensor for highly selective and sensitive detection of bioavailable methylmercury in the environment is constructed. The biosensor carries luciferase gene as a reporter under control of a very selective Hg2+-inducible part of the mer-operon from Pseudomonas K-62 plasmid pMR26. A merB gene encoding organomercurial lyase which cleaves the C-Hg bond of methylmercury to give Hg2+ is coexpressed in the sensor.
environmental protection
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detoxification of organomercury compounds is of critical importance. The bioorganometallic chemistry of mercury in a sulfur-rich coordination environment is studied in order emulate the structure and function of MerB. One of the three non-structural cysteine residues of MerB that are crucial for enzymatic activity is required to coordinate [HgR]+ in a linear manner, a second cysteine is required to activate the Hg-alkyl group toward protolytic cleavage, and the third cysteine is required to effect the cleavage reaction.
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Escherichia coli (P77072), Escherichia coli, Priestia megaterium (Q7DJN2)
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