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Information on EC 4.99.1.2 - alkylmercury lyase
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4.99.1.2 alkylmercury lyaseIUBMB Comments
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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Word Map
- 4.99.1.2
- methylmercury
-
mercury-resistant
-
protonolysis
-
phytoremediation
- phenylmercury
-
hg-resistant
- environmental protection
-
biomagnifies
-
mercury-contaminated
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
organomercurial lyase, merb3, organomercury lyase, merb1, merb2, alkylmercury lyase, 
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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
RHg+ + H+ = RH + Hg2+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
-
-
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
organomercurial salts + H+
?
-
primary, secondary, tertiary, alkyl, vinyl, allyl, aryl
-
-
?
alkyl mercuric halides + H+
?
-
primary, secondary, tertiary
-
-
?
CH3Hg+ + H+
CH4 + Hg2+
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
-
-
?
CH3Hg+ + H+
Hg2+ + CH4
the growth rates of both the wild-type and ppk/merTtransgenic tobacco callus are largely inhibited by CH3Hg+ in a dose-dependent manner
-
-
?
crotonyl mercuric bromide + H+
crotonaldehyde + Hg2+ + Br-
-
-
-
-
?
ethylmercury chloride
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
about 12% organomercury remaining after 24 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
-
about 1% organomercury remaining after 72 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
-
about 13% organomercury remaining after 24 h incubation
-
-
?
ethylmercury chloride
Hg2+ + ?
-
about 13% organomercury remaining after 24 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
about 12% organomercury remaining after 24 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
best substrate, about 5% organomercury remaining after 24 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
-
best substrate, less than 1% organomercury remaining after 72 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
-
about 52% organomercury remaining after 24 h incubation
-
-
?
methylmercury chloride
Hg2+ + ?
-
about 52% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
about 10% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
about 10% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
merB3 gene product
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
about 12% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
about 7% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
about 12% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
about 7% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
about 40% organomercury remaining after 72 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
about 18% organomercury remaining after 24 h incubation
-
-
?
p-chloromercuribenzoate
Hg2+ + p-hydroxybenzoate
-
about 18% organomercury remaining after 24 h incubation
-
-
?
phenyl mercuric acetate + H+
benzene + Hg2+ + acetate
-
-
-
?
phenylmercury acetate
?
about 45% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
about 45% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
about 50% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
about 65% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
about 50% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
about 65% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
-
about 65% organomercury remaining after 72 h incubation
-
-
?
phenylmercury acetate
?
-
about 55% organomercury remaining after 24 h incubation
-
-
?
phenylmercury acetate
?
-
about 55% organomercury remaining after 24 h incubation
-
-
?
thimerosal
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
thimerosal
Hg2+ + ?
about 10% organomercury remaining after 24 h incubation
-
-
?
thimerosal
Hg2+ + ?
about 12% organomercury remaining after 24 h incubation
-
-
?
thimerosal
Hg2+ + ?
about 7% organomercury remaining after 24 h incubation
-
-
?
thimerosal
Hg2+ + ?
-
about 3% organomercury remaining after 72 h incubation
-
-
?
thimerosal
Hg2+ + ?
-
about 13% organomercury remaining after 24 h incubation
-
-
?
thimerosal
Hg2+ + ?
-
about 13% organomercury remaining after 24 h incubation
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CH3Hg+ + H+
CH4 + Hg2+
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
-
-
?
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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
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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
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
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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
-
coexpression of enzyme and mercuric reductase in Arabidopsis thaliana leads to growth on 50fold higher methylmercury concentrations than wild type plants
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
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
-
coexpression of enzyme and mercuric reductase in Arabidopsis thaliana leads to growth on 50fold higher methylmercury concentrations than wild-type plants
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
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
-
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
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walsh, C.; Begley, T.; Walts, A.
Bacterial organomercurial lyase: Mechanistic studies on a protonolytic organomercurial cleaving enzyme in mercurial detoxification
Stereochem. Org. Bioorg. Transform. (Proc. Workshop, Conf. Hoechst,17th Meeting, Bartmann, W. , Sharpless, K. , eds. )
17
73-83
1986
Escherichia coli, Escherichia coli overproducing
-
brenda
Walts, A.; Walsh, C.T.
Bacterial organomercurial lyase: Novel enzymatic protonolysis of organostannanes
J. Am. Chem. Soc.
110
1950-1953
1988
Escherichia coli
-
brenda
Begley, T.P.; Walts, A.E.; Walsh, C.T.
Mechanistic studies of a protonolytic organomercurial cleaving enzyme: bacterial organomercurial lyase
Biochemistry
25
7192-7200
1986
Escherichia coli
brenda
Begley, T.P.; Walts, A.E.; Walsh, C.T.
Bacterial organomercurial lyase: overproduction, isolation, and characterization
Biochemistry
25
7186-7192
1986
Escherichia coli
brenda
Tezuka, T.; Tonomura, K.
Purification and properties of an enzyme catalyzing the splitting of carbon-mercury linkages from mercury-resistant Pseudomonas K-62 strain. I. Splitting enzyme 1
J. Biochem.
80
79-87
1976
Pseudomonas sp.
brenda
Griffin, H.G.; Foster, T.J.; Silver, S.; Misra, T.K.
Cloning and DNA sequence of the mercuric- and organomercurial-resistance determinants of plasmid pDU1358
Proc. Natl. Acad. Sci. USA
84
3112-3116
1987
Escherichia coli
brenda
Tezuka, T.; Takasaki, Y.
Biodegradation of phenylmercuric acetate by organomercury-resistant Penicillum sp. MR-2
Agric. Biol. Chem.
52
3183-3185
1988
Penicillium sp., Penicillium sp. MR-2
-
brenda
Izaki, K.; Aoki, T.; Takahashi, H.
Degradation of organomercurials in Becillus cereus
Agric. Biol. Chem.
49
2413
1985
Bacillus cereus
-
brenda
Laddaga, R.A.; Chu, L.; Misra, T.K.; Silver, S.
Nucleotide sequence and expression of the mercurial-resistance operon from Staphylococcus aureus plasmid pI258
Proc. Natl. Acad. Sci. USA
84
5106-5110
1987
Staphylococcus aureus, Serratia sp.
brenda
Gachhui, R.; Chaudhuri, J.; Ray, S.; Pahan, K.; Mandal, A.
Studies on mercury-detoxicating enzymes from a broad-spectrum mercury-resistant strain of Flavobacterium rigense
Folia Microbiol. (Praha)
42
337-343
1997
Flavobacterium rigense
brenda
Pahan, K.; Gachhui, R.; Ray, S.; Chaudhuri, J.; Mandal, A.
A PMA degrading constitutive organomercurial lyase in a broad-spectrum mercury resistant Bacillus pasteurii strain DR2
Indian J. Exp. Biol.
29
1147-1149
1991
Sporosarcina pasteurii
brenda
Pahan, K.; Ray, S.; Gachhui, R.; Chaudhuri, J.; Mandal, A.
Effect of thiol compounds and flavins on mercury and organomercurial degrading enzymes in mercury resistant aquatic bacteria
Bull. Environ. Contam. Toxicol.
44
216-223
1990
Alcaligenes faecalis, Sporosarcina pasteurii
brenda
Pahan, K.; Ghosh, D.K.; Ray, S.; Gachhui, R.; Chaudhuri, J.; Mandal, A.
Mercury and organomercurial degrading enzymes in a broad-spectrum Hg-resistant strain of Bacillus pasteurii
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Sporosarcina pasteurii
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Pitts, K.E.; Summers, A.O.
The roles of thiols in the bacterial organomercurial lyase (MerB)
Biochemistry
41
10287-10296
2002
Serratia marcescens
brenda
Huang, C.C.; Narita, M.; Yamagata, T.; Endo, G.
Identification of three merB genes and characterization of a broad-spectrum mercury resistance module encoded by a class II transposon of Bacillus megaterium strain MB1
Gene
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361-366
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Priestia megaterium (Q7DJN2), Priestia megaterium
brenda
Bizily, S.P.; Rugh, C.L.; Meagher, R.B.
Phytodetoxification of hazardous organomercurials by genetically engineered plants
Nat. Biotechnol.
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Escherichia coli
brenda
Bizily, S.P.; Kim, T.; Kandasamy, M.K.; Meagher, R.B.
Subcellular targeting of methylmercury lyase enhances its specific activity for organic mercury detoxification in plants
Plant Physiol.
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Escherichia coli
brenda
Benison, G.C.; Di Lello, P.; Shokes, J.E.; Cosper, N.J.; Scott, R.A.; Legault, P.; Omichinski, J.G.
A stable mercury-containing complex of the organomercurial lyase MerB: catalysis, product release, and direct transfer to MerA
Biochemistry
43
8333-8345
2004
Escherichia coli
brenda
Murtaza, I.; Dutt, A.; Mushtaq, D.; Ali, A.
Molecular cloning and genetic analysis of functional merB gene from indian isolates of Escherichia coli
Curr. Microbiol.
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Escherichia coli (Q9S4I1), Escherichia coli (Q9S4I2), Escherichia coli (Q9S4I3), Escherichia coli
brenda
Taubner, L.M.; McGuirl, M.A.; Dooley, D.M.; Copie, V.
Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein
Biochemistry
45
12240-12252
2006
Achromobacter cycloclastes
brenda
Che, D.; Meagher, R.B.; Rugh, C.L.; Kim, T.; Heaton, A.C.; Merkle, S.A.
Expression of organomercurial lyase in eastern cottonwood enhances organomercury resistance
In Vitro Cell. Dev. Biol. Plant
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228-234
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Populus deltoides
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brenda
Melnick, J.G.; Parkin, G.
Cleaving mercury-alkyl bonds: a functional model for mercury detoxification by MerB
Science
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Escherichia coli, Escherichia coli R831b
brenda
Kotrba, P.; Najmanova, J.; Macek, T.; Ruml, T.; Mackova, M.
Genetically modified plants in phytoremediation of heavy metal and metalloid soil and sediment pollution
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Escherichia coli, Escherichia coli Tn21
brenda
Lafrance-Vanasse, J.; Lefebvre, M.; Di Lello, P.; Sygusch, J.; Omichinski, J.G.
Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation
J. Biol. Chem.
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Escherichia coli (P77072)
brenda
Nagata, T.; Morita, H.; Akizawa, T.; Pan-Hou, H.
Development of a transgenic tobacco plant for phytoremediation of methylmercury pollution
Appl. Microbiol. Biotechnol.
87
781-786
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Pseudomonas sp. K-62 (O07303)
brenda
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
J. Am. Chem. Soc.
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13278-13285
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Escherichia coli (P77072)
brenda
Nagata, T.; Muraoka, T.; Kiyonoa, M.; Pan-Hou, H.
Development of a luminescence-based biosensor for detection of methylmercury
J. Toxicol. Sci.
35
231-234
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Pseudomonas sp. K-62 (O07303)
brenda
Li, X.; Liao, R.Z.; Zhou, W.; Chen, G.
DFT studies of the degradation mechanism of methyl mercury activated by a sulfur-rich ligand
Phys. Chem. Chem. Phys.
12
3961-3971
2010
Escherichia coli (P77072)
brenda
Hong, B.; Nauss, R.; Harwood, I.M.; Miller, S.M.
Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved gamma-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione
Biochemistry
49
8187-8196
2010
Serratia marcescens (P08664)
brenda
Chien, M.F.; Narita, M.; Lin, K.H.; Matsui, K.; Huang, C.C.; Endo, G.
Organomercurials removal by heterogeneous merB genes harboring bacterial strains
J. Biosci. Bioeng.
110
94-98
2010
Staphylococcus aureus, no activity in Bacillus subtilis, Pseudomonas sp., Bacillus cereus (P16172), Priestia megaterium (Q9RHR0), Bacillus cereus RC607 (P16172), Priestia megaterium MB1 (Q9RHR0), no activity in Bacillus subtilis 168, Staphylococcus aureus RN23
brenda
Sone, Y.; Mochizuki, Y.; Koizawa, K.; Nakamura, R.; Pan-Hou, H.; Itoh, T.; Kiyono, M.
Mercurial-resistance determinants in Pseudomonas strain K-62 plasmid pMR68
AMB Express
3
41
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Pseudomonas sp. (I2FG55)
brenda
Mathema, V.B.; Thakuri, B.C.; Sillanpaeae, M.
Bacterial mer operon-mediated detoxification of mercurial compounds: a short review
Arch. Microbiol.
193
837-844
2011
Staphylococcus aureus
brenda
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
Biochemistry
55
1070-1081
2016
Escherichia coli (P77072), Escherichia coli, Priestia megaterium (Q7DJN2)
brenda
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
J. Am. Chem. Soc.
139
910-921
2017
Escherichia coli (P77072), Escherichia coli
brenda
Silva, P.; Rodrigues, V.
Mechanistic pathways of mercury removal from the organomercurial lyase active site
PeerJ
2015
e1127
2015
Escherichia coli (P77072)
brenda
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