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Information on EC 1.16.1.1 - mercury(II) reductase
for references in articles please use BRENDA:EC1.16.1.1
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EC Tree 1 Oxidoreductases
1.16 Oxidizing metal ions
1.16.1 With NAD+ or NADP+ as acceptor
1.16.1.1 mercury(II) reductase
IUBMB Comments
A dithiol enzyme.
The enzyme appears in viruses and cellular organisms
- 1.16.1.1
-
organomercurial
-
mercury-resistant
- hgcl2
- methylmercury
- lipoamide
-
phytoremediation
-
mercury-contaminated
- ferrooxidans
-
hg-resistant
-
geothermal
-
metal-resistant
- phenylmercury
-
mercury-polluted
- environmental protection
showSynonyms
mercuric reductase, mercuric ion reductase, mercury reductase, mer a, bacterial mercuric reductase, mera protein, tn501 mera, mercuric (ii) reductase, mercury(ii) reductase, tn501 mercuric ion reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bacterial mercuric reductase
Mer A
-
-
-
-
MerA
mercurate(II) reductase
-
-
-
-
mercuric (II) reductase
mercuric ion reductase
mercuric reductase
mercury reductase
-
-
-
-
Msed_1241
MseMerA
reduced NADP:mercuric ion oxidoreductase
-
-
-
-
reductase, mercurate(II)
-
-
-
-
mercuric ion reductase
-
-
-
-
mercuric ion reductase
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
-
mercuric reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hg + NADP+ + H+ = Hg2+ + NADPH
-
-
-
-
Hg + NADP+ + H+ = Hg2+ + NADPH
FAD mediates the transfer of electrons between NADPH and Hg2+ bound to an adjacent pair of cysteine thiols (C136 and C141) in the buried active site, while a second pair of cysteines (C558 and C559) on the C-terminal tail mediates transfer of Hg2+ from other protein and small molecule thiols in solution to the active site cysteines through a ligand exchange mechanism, structure-function study, overview
-
Hg + NADP+ + H+ = Hg2+ + NADPH
catalytic mechanisms of the flavoprotein MerA, overview
-
Hg + NADP+ + H+ = Hg2+ + NADPH
molecular mechanism of the Hg transfer is analyzed by quantum mechanical/molecular mechanical (QM/MM) calculations, and simulation. The transfer is nearly thermoneutral and passes through a stable tricoordinated intermediate that is marginally less stable than the two end states. For the overall process, Hg2+ is always paired with at least two thiolates and thus is present at both the C-terminal and catalytic binding sites as a neutral complex. Prior to Hg2+ transfer, C141 is negatively charged. As Hg2+ is transferred into the catalytic site, a proton is transferred from C136 to C559' while C558' becomes negatively charged, resulting in the net transfer of a negative charge over a distance of about 7.5 A. Thus, the transport of this soft divalent cation is made energetically feasible by pairing a competition between multiple Cys thiols and/or thiolates for Hg2+ with a competition between the Hg2+ and protons for the thiolates. Reaction mechansim, detailed overview
-
Hg + NADP+ + H+ = Hg2+ + NADPH
MerA possesses metallochaperone-like N-terminal domains (NmerA) tethered to its catalytic core domain by linkers. The NmerA domains interacts principally through electrostatic interactions with the core, leashed by the linkers so as to subdiffuse on the surface over an area close to the core C-terminal Hg(II)-binding cysteines
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phenylmercury acetate degradation
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SYSTEMATIC NAME
IUBMB Comments
Hg:NADP+ oxidoreductase
A dithiol enzyme.
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CAS REGISTRY NUMBER
COMMENTARY
67880-93-7
-
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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
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
Hg + NADP+ + H+
Hg2+ + NADPH
-
Substrates: -
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
Substrates: MerA catalyzes the bioconversion of toxic Hg2+ to the least toxic elemental Hg0, and is capable of reducing the Hg2+, via NADPH as an electron donor
Products: -
Products: -
?
Hg + NADP+ + H+
Hg2+ + NADPH
A8UT36
Substrates: -
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
-
Substrates: Cys11 and Cys14 are involved in metal binding, role for Tyr62 in modulating the pKa values of the cysteine thiols
Products: -
Products: -
?
Hg + NADP+ + H+
Hg2+ + NADPH
-
Substrates: the enzmye reduces reactive Hg2+ to volatile and relatively inert monoatomic Hg0 vapor. Pseudomonas putida SP1 is able to volatilize almost 100% of the total mercury it is exposed to
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
-
Substrates: the enzmye reduces reactive Hg2+ to volatile and relatively inert monoatomic Hg0 vapor. Pseudomonas putida SP1 is able to volatilize almost 100% of the total mercury it is exposed to
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
Substrates: organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview
Products: -
Products: -
?
Hg2+ + NADH
Hg + NAD+ + H+
-
Substrates: nearly identical activity with NADPH or NADH
Products: -
Products: -
?
Hg2+ + NADH
Hg + NAD+ + H+
-
Substrates: very little activity with NADH
Products: -
Products: -
?
Hg2+ + NADH
Hg + NAD+ + H+
-
Substrates: very little activity with NADH
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: last step in bacterial mercury detoxification pathway
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense
-
Substrates: mercury resistance is due to the sequential action of two mercury-detoxificating enzymes, organomercurial lyase and mercuric reductase. Enzyme is induced by Hg2+ and organomercurials
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense PR2
-
Substrates: mercury resistance is due to the sequential action of two mercury-detoxificating enzymes, organomercurial lyase and mercuric reductase. Enzyme is induced by Hg2+ and organomercurials
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: nearly identical activity with NADPH or NADH
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: the enzyme is a key component of an organomercurial detoxification system
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: the enzyme is a key component of an organomercurial detoxification system
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Substrates: the merA mutant exhibits mercury sensitivity relative to wild type and is defective in elemental mercury volatilization
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Yersinia enterolytica 138A14
-
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: key enzyme in detoxification of mercury in bacteria
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: mercuric ion resistance in bacteria requires transport of Hg2+ ions into the cytoplasmic compartment where they are reduced to the less toxic metallic mercury Hg0 by mercuric reductase
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: interactions between the inner membrane mercuric ion transporter, MerT, and the N-terminal domain of cytoplasmic mercuric reductase, transport is the rate-limiting step in mercury detoxification, overview
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: key enzyme in detoxification of mercury in bacteria
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: key enzyme in detoxification of mercury in bacteria
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: Tyr264 and Tyr605 are involved in substrate binding, Tyr264 is important for catalysis, possibly by destabilizing the binding of Hg(II) to the two ligating thiolates at the active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: Tyr264 and Tyr605 are involved in substrate binding, Tyr264 is important for catalysis, possibly by destabilizing the binding of Hg(II) to the two ligating thiolates at the active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: Cys558 plays a more important role in forming the reducible complex with Hg(II), while both Cys558 and Cys559 seem to be involved in efficient scavenging of Hg(II)
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-function study of the N-terminal HMA domain NmerA of Tn501 mercuric ion reductase , i.e. MerA, using NMR and spectral techniques, overview. Determination of NMR solution structures of reduced and Hg2+-bound forms of NmerA
Products: -
Products: -
?
additional information
?
-
-
Substrates: Pseudomonas sp. strain B50A exhibiting Mercuric (II) reductase activity removes 86% of the mercury present in the culture medium. ENzyme activity is measured as capacity to remove mercury from the growth medium, activity profile for Pseudomonas sp. B50A, overview
Products: -
Products: -
?
additional information
?
-
Substrates: proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview
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
Hg + NADP+ + H+
Hg2+ + NADPH
Substrates: MerA catalyzes the bioconversion of toxic Hg2+ to the least toxic elemental Hg0, and is capable of reducing the Hg2+, via NADPH as an electron donor
Products: -
Products: -
?
Hg + NADP+ + H+
Hg2+ + NADPH
A8UT36
Substrates: -
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
-
Substrates: the enzmye reduces reactive Hg2+ to volatile and relatively inert monoatomic Hg0 vapor. Pseudomonas putida SP1 is able to volatilize almost 100% of the total mercury it is exposed to
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
-
Substrates: the enzmye reduces reactive Hg2+ to volatile and relatively inert monoatomic Hg0 vapor. Pseudomonas putida SP1 is able to volatilize almost 100% of the total mercury it is exposed to
Products: -
Products: -
r
Hg + NADP+ + H+
Hg2+ + NADPH
Substrates: organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: last step in bacterial mercury detoxification pathway
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense
-
Substrates: mercury resistance is due to the sequential action of two mercury-detoxificating enzymes, organomercurial lyase and mercuric reductase. Enzyme is induced by Hg2+ and organomercurials
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense PR2
-
Substrates: mercury resistance is due to the sequential action of two mercury-detoxificating enzymes, organomercurial lyase and mercuric reductase. Enzyme is induced by Hg2+ and organomercurials
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
Substrates: -
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: the enzyme is a key component of an organomercurial detoxification system
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: the enzyme is a key component of an organomercurial detoxification system
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
Substrates: the merA mutant exhibits mercury sensitivity relative to wild type and is defective in elemental mercury volatilization
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
Substrates: inducible enzyme
Products: -
Products: -
?
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: key enzyme in detoxification of mercury in bacteria
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: mercuric ion resistance in bacteria requires transport of Hg2+ ions into the cytoplasmic compartment where they are reduced to the less toxic metallic mercury Hg0 by mercuric reductase
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: key enzyme in detoxification of mercury in bacteria
Products: -
Products: -
r
Hg2+ + NADPH
Hg(0) + NADP+
-
Substrates: key enzyme in detoxification of mercury in bacteria
Products: -
Products: -
r
additional information
?
-
-
Substrates: Pseudomonas sp. strain B50A exhibiting Mercuric (II) reductase activity removes 86% of the mercury present in the culture medium. ENzyme activity is measured as capacity to remove mercury from the growth medium, activity profile for Pseudomonas sp. B50A, overview
Products: -
Products: -
?
additional information
?
-
Substrates: proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
a flavoprotein, spectral analysis of the binding structure and environment, overview
FAD
-
flavoprotein. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts
NADPH
-
in the presence of an excess of NADPH, the final product of the reaction is probably an NADPH complex of two-electron-reduced enzyme, but below pH 6 the final spectrum becomes less intense suggesting a partial formation of four-electron-reduced enzyme
NADPH
-
in presence of 1 mM cysteine only one equivalent of NADPH per FAD is required for full activation
NADPH
-
the first two steps of the reaction involve 1 mol NADPH per mol FAD, the third requires a second equivalent of NADPH
additional information
the enzymes contains FAD, utilizes NADPH as an electron donor, and requires an excess of exogenous thiols for activity
-
additional information
-
each monomer contains a FAD and a redoxactive disulfide group close to the FAD isoalloxazine ring. MerA has an additional Cys/Cys redox site in the C-terminal part of its sequence
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
0.1 mM of Cr6+ and Fe3+ do not have significant effect on the enzyme activity
additional information
-
0.1 mM of Cr6+ and Fe3+ do not have significant effect on the enzyme activity
additional information
-
the organism is resistant to CdCl2, CoCl2, CrCl3, CuCl2, PbCl2, ZnSO4, and to 0.28 mM HgCl2
additional information
-
ions Sn2+, Ni2+ and Cd2+ neither inhibit nor stimulate the enzyme activity
additional information
the mercuric reductase is functional in high salt and resistant to high concentrations of Hg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
substrate inhibition of the reaction with 2,4,6-trinitrobenzenesulfonate and NADPH
NaCl
A0A2H4QUB4
isoform K35NH is strongly inhibited by NaCl, retaining 36% and 13.7% of its maximum activity (in the absence of NaCl) at concentrations of 2.0 M and 4.0 M NaCl, respectively
NaCl
isoform ATII-LCL-NH shows 55% residual activity at 0.5 M NaCl
additional information
Enterobacter sp. A25B
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
additional information
Enterobacter sp. B50C
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
additional information
-
no inhibition by 2,4,6-trinitrobenzenesulfonate; not inhibitory: 0.1 mM NADP+; not inhibitory: 100 microM 2,4,6-trinitrobenzenesulfonate
-
additional information
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
additional information
-
the organism is highly resistant to the antibiotics ampicillin, kanamycin, chloramphenicol, and tetracycline
-
additional information
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
additional information
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
additional information
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
additional information
-
determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
A0A2H4QUB4
isoform K09H is activated by NaCl, reaching its maximum activity at 2.0 M NaCl, an 1.8fold increase relative to its activity in the absence of NaCl
NADPH
-
100 microM, 30 min preincubation, relative initial rate 151%, 10 min preincubation with NADPH results in an increase of reactive thiol groups
thiol
-
exogenous thiols are required for catalytic reduction of Hg(II) to Hg2+, due to prevention or reversal of formation of an abortive complex of Hg(II) with the thiol/thiolate pair of two-electron reduced enzyme
additional information
-
0.1 mM NADP+ stimulates the 2,4,6-trinitrobenzenesulfonate-dependent NADPH oxidation more than 10fold
-
2-mercaptoethanol
-
thiol compound required, optimal concentration is 0.5 mM
NADP+
-
strong stimulation of the reaction with 2,4,6-trinitrobenzenesulfonate and NADPH
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Chemotherapy vs. chemoimmunotherapy with methanol extraction residue of Bacillus Calmette-Guerin (MER) in advanced breast cancer: a randomized trial by the Piedmont Oncology Association.
Hypersensitivity
Deletions in the r-determinant mer region of plasmid R100-1 selected for loss of mercury hypersensitivy.
Hypersensitivity
Organomercurial resistance determinants in Pseudomonas K-62 are present on two plasmids.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01096
Hg2+
isoform ATII-LCL-NH mutant D415A/D416A, at 25°C, pH not specified in the publication
0.01125
Hg2+
isoform ATII-LCL-NH, at 25°C, pH not specified in the publication
0.0139
Hg2+
isoform ATII-LCL-NH mutant D414A/D415A/D416A/D417A, at 25°C, pH not specified in the publication
0.035
Hg2+
-
recombinant catalytic core, presence of N-terminal sequence NmerA, 25°C, pH 7.3
additional information
additional information
Yersinia enterolytica
-
the Km-value for HgCl2 is dependent on the concentration of exogenous thiol compounds
-
additional information
additional information
steady-state kinetic analysis, overview, apparent second-order rate constant for Hg(II) transfer from MerB to NmerA
-
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
Hg2+
-
recombinant catalytic core, presence of N-terminal sequence NmerA, 25°C, pH 7.3
12
Hg2+
isoform ATII-LCL-NH mutant D415A/D416A, at 25°C, pH not specified in the publication
12.25
Hg2+
isoform ATII-LCL-NH, at 25°C, pH not specified in the publication
12.6
Hg2+
isoform ATII-LCL-NH mutant D414A/D415A/D416A/D417A, at 25°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
cell extract, mercury-dependent oxidation of NADPH, pH 7.4, 25°C
1.9
NADPH oxidation-linked Hg2+ reduction specific activity, purified recombinant His-tagged enzyme, pH 6.7, 37°C
10.95
isoform ATII-LCL-NH mutant D415A/D416A, at 25°C, pH not specified in the publication
10.96
isoform ATII-LCL-NH, at 25°C, pH not specified in the publication
11.1
isoform ATII-LCL-NH mutant D414A/D415A/D416A/D417A, at 25°C, pH not specified in the publication
3.1
NADPH oxidation-linked Hg2+ reduction specific activity, purified recombinant His-tagged enzyme, pH 6.7, 70°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
6.5 - 9
-
pH 6.5: about 60% of maximal activity, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
37 - 70
assay at, enzyme activity at 70°C is about 1.6fold higher compared to activity at 37°C
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from surface and sub-surface floodplain soil, Oak Ridge, USA, gene merA
-
-
brenda
Enterobacter sp. A25B
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
Enterobacter sp. B50C
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
isolated from Pisciarelli Solfatara in Naples, Italy
UniProt
brenda
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
isolated from Pisciarelli Solfatara in Naples, Italy
UniProt
brenda
mercury-resistant Escherichia coli strain containing plasmid R100 encoding gene merA in the mer operon
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
Pseudomonas entomophila B100A
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
marine-isolated mercury-resistant strain, isolated from seawater collected from Yantai coastal zone in Shandong Province, China, gene merA encoded in the mer operon
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
isolated from surface and sub-surface floodplain soil, Oak Ridge, USA, gene merA
-
-
brenda
isolated from surface and sub-surface floodplain soil, Oak Ridge, USA, gene merA
-
-
brenda
from the unique deep brine environment of Atlantis II in the Red Sea, lower convective layer, gene merA
UniProt
brenda
enzyme encoded by Tn5044 merA gene, thermosensitive resistance to mercury, expression and functional activity of enzyme are severely inhibited at 37-41.5°C
-
-
brenda
plasmid R100; Escherichia coli containing plasmid R100 encoding gene merA
UniProt
brenda
i.e. Bacillus sphaericus, isolated from an industrial mercuric salt-contaminated soil, gene merA
UniProt
brenda
i.e. Bacillus sphaericus, isolated from an industrial mercuric salt-contaminated soil, gene merA
UniProt
brenda
possessing the Tn501 plasmid, a transposon determining resistance to mercuric ions
-
-
brenda
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury
-
-
brenda
marine-isolated mercury-resistant strain, isolated from seawater collected from Yantai coastal zone in Shandong Province, China, gene merA encoded in the mer operon
-
-
brenda
analysis of enzyme in several thermophylic crenarchaeal and gram-positive taxa isolates from a hot spring. An essential role for mercuric reductase is evident during growth in the mercury-contaminated environment. Despite environmental selection for mercury resistance and the proximity of community members, the enzyme retains the two distinct prokaryotic forms and avoids genetic homogenization
-
-
brenda
probably a betaproteobacterium or a gammaproteobacterium
A0A2H4QUB4
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
A8UT36
strain R1-1 is resistant to concentration of over 0.01 mM Hg2+, transforms Hg(II) to Hg(0) during cellular growth, and possesses Hg-dependent NAD(P)H oxidation activities in crude cell extracts that are optimal at temperatures corresponding with the strains' optimal growth temperature of 70°C
brenda
additional information
B4U9T7
strain AAS1 is resistant to concentration over 0.01 mM Hg2+, transforms Hg(II) to Hg(0) during cellular growth, and possesses Hg-dependent NAD(P)H oxidation activities in crude cell extracts that are optimal at temperatures corresponding with the strains' optimal growth temperature of 55°C
brenda
additional information
growth of strain G1 at sublethal concentrations of metal salts, Cd2+, Zn2+, Co2+, and K2Cr2O7-, in presence of absence of Hg2+, overview
brenda
additional information
-
growth of strain G1 at sublethal concentrations of metal salts, Cd2+, Zn2+, Co2+, and K2Cr2O7-, in presence of absence of Hg2+, overview
brenda
additional information
-
growth of strain G1 at sublethal concentrations of metal salts, Cd2+, Zn2+, Co2+, and K2Cr2O7-, in presence of absence of Hg2+, overview
-
brenda
additional information
Metallosphaera sedula is isolated from Pisciarelli Solfatara in Naples, Italy. Pisciarelli Solfatara contains a variety of thermal features that range in temperature from about 30°C to nearly 100°C, and a pH range of pH 1.5 to around pH 6.0 with elevated concentrations of heavy metals, including Hg2+ at concentrations up to 0.005g/kg
brenda
additional information
-
Metallosphaera sedula is isolated from Pisciarelli Solfatara in Naples, Italy. Pisciarelli Solfatara contains a variety of thermal features that range in temperature from about 30°C to nearly 100°C, and a pH range of pH 1.5 to around pH 6.0 with elevated concentrations of heavy metals, including Hg2+ at concentrations up to 0.005g/kg
brenda
additional information
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
Metallosphaera sedula is isolated from Pisciarelli Solfatara in Naples, Italy. Pisciarelli Solfatara contains a variety of thermal features that range in temperature from about 30°C to nearly 100°C, and a pH range of pH 1.5 to around pH 6.0 with elevated concentrations of heavy metals, including Hg2+ at concentrations up to 0.005g/kg
-
brenda
additional information
-
the low virulence strain is part of the biofilm. Optimal pH for the growth and enzyme activity of strain SP1 in presence of HgCl2 is pH 8.0-9.0, whereas optimal pH for expression of merA is pH 5.0
brenda
additional information
-
the low virulence strain is part of the biofilm. Optimal pH for the growth and enzyme activity of strain SP1 in presence of HgCl2 is pH 8.0-9.0, whereas optimal pH for expression of merA is pH 5.0
-
brenda
additional information
the organism is grown in the lower convective layer of the brine pool at Atlantis II Deep in the Red Sea, with a maximum depth of over 2000 m, the pool is characterized by acidic pH 5.3, high temperature 68°C, , salinity of 26%, low light levels, anoxia, and high concentrations of heavy metals
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
evolution
physiological function
additional information
evolution
organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview. Hg(II) removal from MerB by the N-terminal domain, NmerA, and catalytic core C-terminal cysteine pairs of its coevolved MerA and by GSH, the major competing cellular thiol in gamma-proteobacteria. The reaction with a 10fold excess of NmerA over HgMerB removes about 92% of Hg(II), while similar extents of reaction require more than 1000fold excess of GSH
evolution
MerA is part of the disulfide oxidoreductase (DSOR) family, are ancient enzymes that have arisen in high temperature environments after the great oxidation event about 2.4 billion years ago
evolution
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
MerA is part of the disulfide oxidoreductase (DSOR) family, are ancient enzymes that have arisen in high temperature environments after the great oxidation event about 2.4 billion years ago
-
physiological function
organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview. Hg(II) removal from MerB by the N-terminal domain, NmerA, and catalytic core C-terminal cysteine pairs of its coevolved MerA and by GSH, the major competing cellular thiol in gamma-proteobacteria. The reaction with a 10fold excess of NmerA over HgMerB removes about 92% of Hg(II), while similar extents of reaction require more than 1000fold excess of GSH. NmerA reacts more completely than GSH with HgMerB
physiological function
MerA catalyzes the bioconversion of toxic Hg2+ to the least toxic elemental Hg0
physiological function
the mercuric reductase is functional in high salt, stable at high temperatures, resistant to high concentrations of Hg2, and efficiently detoxifies Hg2 in vivo. Mercuric ion reductase catalyzes the reduction of Hg2+ to Hg0, which is volatile and can be disposed of nonenzymatically
physiological function
-
the enzyme catalyzes the reduction and detoxification of toxic mercuric ion, it reduces the Hg(II) ion to the less toxic elemental mercury (Hg(0)) using NADPH as a source of reducing power
physiological function
-
MerB-mediated MeHg demethylation is dependent on the presence of the enzyme
physiological function
-
MerB-mediated MeHg demethylation is dependent on the presence of the enzyme
-
additional information
-
comparison of structural changes upon metal binding in normally appended metal binding proteins: NmerA with and without Hg2+ , PDB entry 2KT3 and 2KT2, respectively
additional information
-
MerA is an inducible NADPH-dependent and flavin containing disulfide oxidoreductase enzyme. MerA-encoding plasmid R100-containing Escherichia coli strains are involved in environmental inorganic mercury detoxification
additional information
the two acidic residues immediately adjacent to the NmerA metal-binding motif in the ATII-LCL protein have a direct effect on both the halophilicity and catalytic efficiency of the enzyme. Presumably, by increasing the efficiency of delivery of Hg2 ions to the catalytic core for reduction, they also help the host to cope with the high concentrations of mercury present in its hypersaline environment
additional information
A8UT36
strain R1-1 is resistant to concentration of over 0.01 mM Hg2+, transforms Hg(II) to Hg(0) during cellular growth, and possesses Hg-dependent NAD(P)H oxidation activities in crude cell extracts that are optimal at temperatures corresponding with the strains' optimal growth temperature of 70°C
additional information
-
many MerA proteins possess metallochaperone-like N-terminal domains (NmerA) that can transfer Hg2+ to the catalytic core domain (Core) for reduction to Hg0. These domains are tethered to the homodimeric core by an about 30-residue linkers that are susceptible to proteolysis, interactions of NmerA and the Core in the full-length protein, structure homology modelling amd structure-function analysis, detailed overview. Binding of Hg2+ to MerA does not alter its hydrodynamic volume
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
Enterobacter sp. B50C
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
Enterobacter sp. A25B
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the resonance Raman (RR) spectra of various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts
additional information
-
molecular mechanism of the Hg transfer is analyzed by quantum mechanical/molecular mechanical (QM/MM) calculations. The transfer is nearly thermoneutral and passes through a stable tricoordinated intermediate that is marginally less stable than the two end states. For the overall process, Hg2+ is always paired with at least two thiolates and thus is present at both the C-terminal and catalytic binding sites as a neutral complex. Prior to Hg2+ transfer, C141 is negatively charged. As Hg2+ is transferred into the catalytic site, a proton is transferred from C136 to C559' while C558' becomes negatively charged, resulting in the net transfer of a negative charge over a distance of about 7.5 A. Thus, the transport of this soft divalent cation is made energetically feasible by pairing a competition between multiple Cys thiols and/or thiolates for Hg2+ with a competition between the Hg2+ and protons for the thiolates. Reaction mechansim, formation of a tri-coordinated intermediate state, INT-III, detailed overview
additional information
-
full-length MerA homodimer structure and transfer of Hg(II) from the solvent into the catalytic sites of the MerA core, overview. Enzyme structure-function analysis by molecular dynamics, coarse-grained simulations, small-angle neutron scattering, neutron spin-echo spectroscopy, and dynamic light scattering
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
Pseudomonas entomophila B100A
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
-
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
-
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
-
Show AA Sequence and Transmembrane Helices (2738 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
190000
54000
56000
58000
62000
69000
additional information
additional information
-
nucleotide sequence of the gene encoding mercuric reductase
additional information
-
the enzyme shows extensive sequence homology and functional similarities in the active site of mercuric reductase and nicotinamide disulfide oxidoreductase
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
trimer
additional information
dimer
Enterobacter sp. A25B
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
Enterobacter sp. B50C
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
-
dimer
Pseudomonas entomophila B100A
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
-
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
-
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
homodimer
2 * 60000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
interfacial active site of the MerA homodimer, structure overview
homodimer
each monomer contributes one active site, made up of a pair of redox-active cysteines, to a catalytic core located at the dimer interface, three-dimensional structure homology modeling, overview
trimer
Yersinia enterolytica 138A14
-
3 * 70000, SDS-PAGE
-
additional information
-
N-terminal domain NmerA participates in acquisition and delivery of Hg2+ to the catalytic core during thr reduction catalyzed by full-length enzyme
additional information
-
N-terminal domain NmerA participates in acquisition and delivery of Hg2+ to the catalytic core during thr reduction catalyzed by full-length enzyme
-
additional information
structure comparison of wild-type with mutant Tn501 MerA, PDB ID 1ZK7
additional information
-
structure comparison of wild-type with mutant Tn501 MerA, PDB ID 1ZK7
additional information
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
structure comparison of wild-type with mutant Tn501 MerA, PDB ID 1ZK7
-
additional information
-
structure comparisons of the mutant C136A/C141A (AACC) Hg2+/NADP+ complex (PDB 4K7Z) and the oxidized wild-type (CCCC) enzyme (PDB 1ZK7)
additional information
Yersinia enterolytica
-
along with ageing, as well as limited proteolytic digestion, the enzyme evolves to give a dimeric molecule of 105000 Da composed of two identical subunits of 52000 Da
additional information
Yersinia enterolytica 138A14
-
along with ageing, as well as limited proteolytic digestion, the enzyme evolves to give a dimeric molecule of 105000 Da composed of two identical subunits of 52000 Da
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, mixing of 10 mg/ml protein in 50 mM phosphate buffer, pH 7.2, with reservoir solution containing 5% v/v Tascimate, 0.1 M HEPES, pH 7.0, and 10% w/v PEG monomethyl ether 5000, X-ray diffraction structure determination and analysis at 3.48 A resolution
purified recombinanat His-tagged enzyme, vapour diffusion hanging drop method, from 0.085 M Tris, pH 8.5, 15% v/v glycerol, 14% w/v PEG 400, 0.19 M LiSO4, and 20 mg/ml protein, 2 weeks, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement using Tn501 MerA, PDB ID 1ZK7, as template, modeling
purified recombinanat His-tagged enzyme Tn501 MerA, as NADP+/Hg2+ complex of mutant C136A/C141A, hanging drop vapor diffusion technique, mixing of 0.002 ml of 25 mg/ml protein solution with 0.0.02 ml of reservoir solution containing 0.1 M Tris, pH 9.4, 20 mM NADP+, 2.0 M (NH4)2SO4, equilibration against 0.5 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.6 A resolution, modeling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C628A
-
HgX2 substrates with small ligands can rapidly access the redox-active cysteines in the absence of the C-terminal cysteines, but those with large ligands require the C-terminal cysteines for rapid access. The C-terminal cysteines play a critical role in removing the high-affinity ligands before Hg(II) reaches the redox-active cysteines
C629A
-
HgX2 substrates with small ligands can rapidly access the redox-active cysteines in the absence of the C-terminal cysteines, but those with large ligands require the C-terminal cysteines for rapid access. The C-terminal cysteines play a critical role in removing the high-affinity ligands before Hg(II) reaches the redox-active cysteines
Y264F
-
Km-value for Hg2+ is 5fold lower compared to the Km-value of the wild-type enzyme, turn-over number is reduced by 164fold
Y264F/Y605F
-
Km-value for Hg2+ is 5fold lower than the Km-value of the wild-type enzyme, turnover-number is reduced by 1091fold
Y605F
-
Km-value for Hg2+ is 1.3fold higher compared to the Km-value of the wild-type enzyme, turnover-number is reduced by 6.3fold
C628A
-
HgX2 substrates with small ligands can rapidly access the redox-active cysteines in the absence of the C-terminal cysteines, but those with large ligands require the C-terminal cysteines for rapid access. The C-terminal cysteines play a critical role in removing the high-affinity ligands before Hg(II) reaches the redox-active cysteines
-
C629A
-
HgX2 substrates with small ligands can rapidly access the redox-active cysteines in the absence of the C-terminal cysteines, but those with large ligands require the C-terminal cysteines for rapid access. The C-terminal cysteines play a critical role in removing the high-affinity ligands before Hg(II) reaches the redox-active cysteines
-
Y264F
-
Km-value for Hg2+ is 5fold lower compared to the Km-value of the wild-type enzyme, turn-over number is reduced by 164fold
-
Y264F/Y605F
-
Km-value for Hg2+ is 5fold lower than the Km-value of the wild-type enzyme, turnover-number is reduced by 1091fold
-
Y605F
-
Km-value for Hg2+ is 1.3fold higher compared to the Km-value of the wild-type enzyme, turnover-number is reduced by 6.3fold
-
C558A
-
mutation results in a total disruption of the Hg(II) detoxification pathway in vivo, compared to wild-type enzyme the mutant shows a 20fold reduction in turnover number and a 10fold increase in Km
C559A
-
mutation results in a total disruption of the Hg(II) detoxification pathway in vivo, compared to wild-type enzyme less than a 2fold reduction in turnover number and an increase in Km-value of 4-5fold
Y605H
-
24fold decrease in turnover number and a 15fold decrease in Km-value
E317V/F441Y
C11A
-
site-directed mutagenesis of NmerA residue of the metal binding site
C136A/C141A
-
site-directed mutagenesis, the C136A/C141A catalytic core mutant. Mutation of either C136 or C141 or both results in a total loss of Hg2+ reductase activity. CRystal structure determination with bound substrates
C14A
-
site-directed mutagenesis of NmerA residue of the metal binding site
Y62F
-
site-directed mutagenesis of NmerA residue of the metal binding site
E133G/E134G
site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme
E15A/E16A
site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme
E515A/E516A
site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme
E545A/E546A
site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme
K432L/P433D/A434L/R435T
site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme
K432L/P433D/A434L/R435T/K465D/V466S/G467R/K468T/F469L/P470T
site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme
D414A/D415A/D416A/D417A
the mutations increase the sensitivity of the enzyme to NaCl as compared to the wild type enzyme
D415A/D416A
the mutations enhance the thermal stability of the enzyme which retains 81% of its activity after 10 min of incubation at 70°C
additional information
E317V/F441Y
mutant Tn501 MerA, structure comparison with the wild-type
E317V/F441Y
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
mutant Tn501 MerA, structure comparison with the wild-type
-
additional information
-
cloning and expression of catalytic core and N-terminal domain of enzyme as separate proteins. the N-terminal domain NmerA is a stable, soluble protein that binds 1 Hg2+ per domain and delivers it to the catalytic core at kinetically competent rates
additional information
-
cloning and expression of catalytic core and N-terminal domain of enzyme as separate proteins. the N-terminal domain NmerA is a stable, soluble protein that binds 1 Hg2+ per domain and delivers it to the catalytic core at kinetically competent rates
-
additional information
-
constitutive expression of enzyme in Pseudomonas putida results in a broad spectrum mercury resistance
additional information
mutations to substitute residues from the ATII-LCL MerA to their corresponding amino acids in the soil enzyme, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 70
purified recombinant enzyme, slight loss of activity 60°C, loss of 90% activity at 70°C and above
70
80
97
purified recombinant His-tagged enzyme, pH 6.7, 100 min, activity remaining
additional information
the mercuric reductase is stable at high temperatures
70
isoform ATII-LCL-NH retains 44% of its activity after 10 min of incubation at 70°C
70
isoform ATII-LCL retains 70% of its activity after 10 min of incubation at 70°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization of the enzyme appears to significantly enhance storage stability
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
activated enzyme appears to be stable under anaerobic conditions and eventually returns to the original level of activity in the presence of oxygen. The activated state seems to be stabilized by 1mM cysteine.
-
438069
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM potassium phosphate buffer, pH 7.2, 0.5 mM EDTA, 1% 2-mercaptoethanol, half-life of soluble enzyme is 3 weeks, immobilized enzyme shows large decline at the beginning and almost no further decrease of activity after 3 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography and Superdex 75 gel filtration
purification of the major 14C-labeled peptide from a tryptic digestion of labeled mercuric reductase
-
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis,
recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain BL21(DE3)
recombinant His-tagged MerA from Escherichia coli strain BL21(DE3)Plys by nickel affinity chromatography
-
recombinant MerA catalytic core and NmerA proteins from Escherichia coli strain XL-1 Blue by anion exchange chromatography and gel filtreation, and separation by affinity chromatography
recombinant wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion enzymes from Escherichia coli strain C43 by amylose affinity chromatography, cleavage of the tags by 3C protease, ultrafiltration, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene merA
gene merA and mer operon, expression of MerA catalytic core and NmerA proteins in Escherichia coli strain XL-1 Blue
gene merA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene merA, DNA and amino acid sequence determination and analysis, pylogenetic analysis and tree, recombinant expression in Escherichia coli strain BL21(DE3)
gene merA, expression as wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion proteins with a 3C protease cleavage site in Escherichia coli strain TOP10 and C43
-
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, mer operon located on Tn5041, DNA and amino acid sequence determination and analysis, chromosomal localization, real-time PCR enzyme expression analysis
-
gene merA, overexpression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene merA, recombinant expression in Escherichia coli strain CM037 harbouring the Tn4378 transposon which contains a mer operon of Rm CH34
-
gene merA, recombinant expression in transgenoc Nicotiana tabacum cv. Xanthium plants using gene transfer by Agrobacterium tumefaciens. Transgenic tobacco expressing merA volatilizes significantly more mercury than wild-type plants. Subcloning in Escherichia coli strains DH5alpha and BL21(DE3)
gene merA, the MerA protein is encoded by the mer operon on transposon Tn501, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene Msed_1241, phylogenetic analysis and tree, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3)
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
plasmid transfer to mercury sensitive Escherichia coli strain DH5alpha, overexpression of gene merA as His-tagged protein in Escherichia coli BL21(DE3)Plys cells
-
subcloning and expression in strain TG2, bacterial two hybrid assays are performed in strain BTH101
-
gene merA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
A8UT36
gene merA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
B4U9T7
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
-
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
-
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by Hg
transcriptional level of merA increased 157fold and 255 fold after 30 min after 60 min of incubation with 6 microM HgCl2+, respectively
-
transcriptional level of merA increased 197fold after incubation with 1 microM CdCl2+
-
transcriptional level of merA increased 30fold and 45fold after treatment with 10 microM ZnCl2+ and 30 microM ZnCl2+, respectively
-
transcriptional level of merA increased 6, 10, and 20fold after treatment with 5, 10, and 20 microM CdSO4 2+, respectively
transcriptional level of merA increased 6, 10, and 20fold after treatment with 5, 10, and 20 microM CdSO4 2+, respectively
-
transcriptional level of merA increased 6, 10, and 20fold after treatment with 5, 10, and 20 microM CdSO4 2+, respectively
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
environmental protection
-
application of the immobilized mercuric reductase for continuous treatment of Hg(II)-containing water in a fixed bed reactor
environmental protection
-
detoxification of mercury by immobilized mercuric reductase
environmental protection
-
the organism can potentially be used for bioremediation in marine environments
environmental protection
enzyme MerA is a promising candidate for Hg2+ bioremediation
environmental protection
-
detoxification of mercury by immobilized mercuric reductase
-
environmental protection
-
application of the immobilized mercuric reductase for continuous treatment of Hg(II)-containing water in a fixed bed reactor
-
environmental protection
-
enzyme MerA is a promising candidate for Hg2+ bioremediation
-
environmental protection
-
the organism can potentially be used for bioremediation in marine environments
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Flavobacterium rigense PR2
brenda
Fox, B.; Walsh, C.T.
Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide
J. Biol. Chem.
257
2498-2503
1982
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501
brenda
Rinderle, S.J.; Booth, J.E.; Williams, J.W.
Mercuric reductase from R-plasmid NR1: characterization and mechanistic study
Biochemistry
22
869-876
1983
Escherichia coli
brenda
Kusano, T.; Ji, G.; Inoue, C.; Silver, S.
Constitutive synthesis of a transport function encoded by the Thiobacillus ferrooxidans merC gene cloned in Escherichia coli
J. Bacteriol.
172
2688-2692
1990
Acidithiobacillus ferrooxidans
brenda
Barkay, T.; Gillman, M.; Liebert, C.
Genes encoding mercuric reductases from selected gram-negative aquatic bacteria have a low degree of homology with merA of transposon Tn501
Appl. Environ. Microbiol.
56
1695-1701
1990
Pseudomonas aeruginosa, Stutzerimonas stutzeri, Burkholderia cepacia
brenda
Moore, M.J.; Distefano, M.D.; Walsh, C.T.; Schiering, N.; Pai, E.F.
Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607
J. Biol. Chem.
264
14386-14388
1989
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) RC607
brenda
Tezuka, T.; Someya, J.
Purification and some properties of mercuric reductase from the organomercury-resistant Penicillium sp. MR-2 strain
Agric. Biol. Chem.
54
1551-1552
1990
Penicillium sp., Penicillium sp. MR-2
-
brenda
Olson, G.J.; Porter, F.D.; Rubinstein, J.; Silver, S.
Mercuric reductase enzyme from a mercury-volatilizing strain of Thiobacillus ferrooxidans
J. Bacteriol.
151
1230-1236
1982
Acidithiobacillus ferrooxidans
brenda
Sahlman, L.; Lambeir, A.M.; Lindskog, S.; Dunford, H.B.
The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa
J. Biol. Chem.
259
12403-12408
1984
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501 (pVS1)
brenda
Sahlman, L.; Lindskog, S.
A stopped-flow study of the reaction between mercuric reductase and NADPH
Biochem. Biophys. Res. Commun.
117
231-237
1983
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501
brenda
Bogdanova, E.S.; Mindlin, S.Z.
Two structural types of mercury reductases and possible ways of their evolution
FEBS Lett.
247
333-336
1989
Arthrobacter sp., Bacillus licheniformis, Bacillus sp. (in: firmicutes), Citrobacter sp., Escherichia coli, Kocuria rosea, Lysinibacillus sphaericus, Micrococcus luteus, Mycobacterium sp., Oerskovia sp., Paenibacillus polymyxa, Priestia megaterium, Rhodococcus sp. (in: high G+C Gram-positive bacteria), Staphylococcus aureus, Staphylococcus saprophyticus
brenda
Sandstroem, A.; Lindskog, S.
Activation of mercuric reductase by the substrate NADPH
Eur. J. Biochem.
164
243-249
1987
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO 9501
brenda
Miller, S.M.; Ballou, D.P.; Massey, V.; Williams, C.H.; Walsh, C.T.
Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction
J. Biol. Chem.
261
8081-8084
1986
Escherichia coli
brenda
Nakahara, H.; Schottel, J.L.; Yamada, T.; Miyakawa, Y.; Asakawa, M.; Harville, J.; Silver, S.
Mercuric reductase enzymes from Streptomyces species and group B Streptococcus
J. Gen. Microbiol.
131
1053-1059
1985
Streptococcus agalactiae, Streptomyces coelicolor, Streptomyces coelicolor M130, Streptomyces espinosus, Streptomyces espinosus 5, Streptomyces lividans, Streptomyces lividans 1326, Streptomyces lividans 8
brenda
Booth, J.E.; Williams, J.W.
The isolation of a mercuric ion-reducing flavoprotein from Thiobacillus ferrooxidans
J. Gen. Microbiol.
130
725-730
1984
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans TFI 29
-
brenda
Meissner, P.S.; Falkinham, J.O.
Plasmid-encoded mercuric reductase in Mycobacterium scrofulaceum
J. Bacteriol.
157
669-672
1984
Mycobacterium scrofulaceum
brenda
Blaghen, M.; Lett, M.C.; Vidon, D.J.M.
Mercuric reductase activity in a mercury-resistant strain of Yersinia enterolytica
FEMS Microbiol. Lett.
19
93-96
1983
Yersinia enterolytica, Yersinia enterolytica 138A14
-
brenda
Carlberg, I.C.; Sahlman, L.; Mannervik, B.
The effect of 2,4,6-trinitrobenzenesulfonate on mercuric reductase, glutathione reductase and lipoamide dehydrogenase
FEBS Lett.
180
102-106
1985
Pseudomonas aeruginosa, Escherichia coli, Pseudomonas aeruginosa PAO9501, Pseudomonas aeruginosa PAO 9501
brenda
Bogdanova, E.S.; Mindlin, S.Z.; Kalyaeva, E.S.; Nikiforov, V.G.
The diversity of mercury reductases among mercury-resistant bacteria
FEBS Lett.
234
280-282
1988
Acinetobacter calcoaceticus, Acinetobacter lwoffii, Aeromonas sp., Aquipseudomonas alcaligenes, Bacillus licheniformis, Bacillus sp. (in: firmicutes), Ectopseudomonas mendocina, Erwinia sp., Escherichia coli, Geobacillus stearothermophilus, Kocuria rosea, Lysinibacillus sphaericus, Oerskovia sp., Paenibacillus polymyxa, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas sp., Rhodococcus sp. (in: high G+C Gram-positive bacteria), Staphylococcus aureus, Staphylococcus saprophyticus, Xanthomonas campestris, Xanthomonas sp.
brenda
Fox, B.S.; Walsh, C.T.
Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide
Biochemistry
22
4082-4088
1983
Pseudomonas aeruginosa
brenda
Sahlman, L.; Lambeir, A.M.; Lindskog, S.
Rapid-scan stopped-flow studies of the pH dependence of the reaction between mercuric reductase and NADPH
Eur. J. Biochem.
156
479-488
1986
Pseudomonas aeruginosa
brenda
Inoue, C.; Sugawara, K.; Shiratori, T.; Kusano, T.; Kitagawa, Y.
Nucleotide sequence of the Thiobacillus ferrooxidans chromosomal gene encoding mercuric reductase
Gene
84
47-54
1989
Acidithiobacillus ferrooxidans
brenda
Rennex, D.; Pickett, M.; Bradley, M.
In vivo and in vitro effects of mutagenesis of active site tyrosine residues of mercuric reductase
FEBS Lett.
355
220-222
1994
Escherichia coli
brenda
Anspach, F.B.; Hueckel, M.; Brunke, M.; Schuette, H.; Deckwer, W.D.
Immobilization of mercuric reductase from a Pseudomonas putida strain on different activated carriers
Appl. Biochem. Biotechnol.
44
135-150
1994
Pseudomonas putida, Pseudomonas putida KT2442::mer-73
-
brenda
Blaghen, M.; Vidon, D.J.M.; El Kebbaj, M.S.
Purification and properties of mercuric reductase from Yersinia enterocolitica 138A14
Can. J. Microbiol.
39
193-200
1993
Yersinia enterolytica, Yersinia enterolytica 138A14
brenda
Ghosh, S.; Sadhukhan, P.C.; Chaudhuri, J.; Ghosh, D.K.; Mandal, A.
Purification and properties of mercuric reductase from Azotobacter chroococcum
J. Appl. Microbiol.
86
7-12
1999
Azotobacter chroococcum, Azotobacter chroococcum SS2
-
brenda
Moore, M.J.; Miller, S.M.; Walsh, C.T.
C-Terminal cysteines of Tn501 mercuric ion reductase
Biochemistry
31
1677-1685
1992
Escherichia coli
brenda
Engst, S.; Miller, S.M.
Alternative Routes for Entry of HgX2 into the Active Site of Mercuric Ion Reductase Depend on the Nature of the X Ligands
Biochemistry
38
3519-3529
1999
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) RC607
brenda
Chang, J.S.; Hwang, Y.P.; Fong, Y.M.; Lin, P.J.
Detoxification of mercury by immobilized mercuric reductase
J. Chem. Technol. Biotechnol.
74
965-973
1999
Escherichia coli, Escherichia coli PWS1
-
brenda
Rennex, D.; Cummings, R.T.; Pickett, M.; Walsh, C.T.; Bradley, M.
Role of tyrosine residues in Hg(II) detoxification by mercuric reductase from Bacillus sp. strain RC607
Biochemistry
32
7475-7478
1993
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) RC607
brenda
Zeroual, Y.; Moutaouakkil, A.; Dzairi, F.Z.; Talbi, M.; Chung, P.U.; Lee, K.; Blaghen, M.
Purification and characterization of cytosolic mercuric reductase from Klebsiella pneumoniae
Ann. Microbiol.
53
149-160
2003
Klebsiella pneumoniae
-
brenda
Vetriani, C.; Chew, Y.S.; Miller, S.M.; Yagi, J.; Coombs, J.; Lutz, R.A.; Barkay, T.
Mercury adaptation among bacteria from a deep-sea hydrothermal vent
Appl. Environ. Microbiol.
71
220-226
2005
Alcanivorax sp., Alcanivorax sp. (Q5ILH3), Alcanivorax sp. (Q5ILH4), Alcanivorax sp. (Q5ILH5), Alcanivorax sp. EPR 10, Alcanivorax sp. EPR 5, Alcanivorax sp. EPR 6 (Q5ILH5), Alcanivorax sp. EPR 7 (Q5ILH4), Alcanivorax sp. EPR 8 (Q5ILH3), Halomonas sp., Marinobacter sp., Pseudoalteromonas sp., Pseudoalteromonas sp. (Q5ILH6), Pseudomonas sp.
brenda
Kholodii, G.; Bogdanova, E.
Tn5044-conferred mercury resistance depends on temperature: the complexity of the character of thermosensitivity
Genetica
115
233-241
2002
Escherichia coli
brenda
Simbahan, J.; Kurth, E.; Schelert, J.; Dillman, A.; Moriyama, E.; Jovanovich, S.; Blum, P.
Community analysis of a mercury hot spring supports occurrence of domain-specific forms of mercuric reductase
Appl. Environ. Microbiol.
71
8836-8845
2005
uncultured bacterium
brenda
Ledwidge, R.; Patel, B.; Dong, A.; Fiedler, D.; Falkowski, M.; Zelikova, J.; Summers, A.O.; Pai, E.F.; Miller, S.M.
NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions
Biochemistry
44
11402-11416
2005
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) RC607
brenda
Schneider, M.; Deckwer, W.
Kinetics of mercury reduction by Serratia marcescens mercuric reductase expressed by Pseudomonas putida strains
Eng. Life Sci.
5
415-424
2005
Serratia marcescens
-
brenda
Schelert, J.; Dixit, V.; Hoang, V.; Simbahan, J.; Drozda, M.; Blum, P.
Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption.
J. Bacteriol.
186
427-437
2004
Saccharolobus solfataricus (Q97VD9), Saccharolobus solfataricus
brenda
Schue, M.; Glendinning, K.J.; Hobman, J.L.; Brown, N.L.
Evidence for direct interactions between the mercuric ion transporter (MerT) and mercuric reductase (MerA) from the Tn501 mer operon
Biometals
21
107-116
2008
Escherichia coli K-12
brenda
Oregaard, G.; S?rensen, S.J.
High diversity of bacterial mercuric reductase genes from surface and sub-surface floodplain soil (Oak Ridge, USA)
ISME J.
1
453-467
2007
Actinomycetota, uncultured beta proteobacterium, uncultured Gammaproteobacteria bacterium
brenda
Park, S.; Ely, R.L.
Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals
Appl. Environ. Microbiol.
74
5475-5482
2008
Nitrosomonas europaea
brenda
Radniecki, T.S.; Semprini, L.; Dolan, M.E.
Expression of merA, amoA and hao in continuously cultured Nitrosomonas europaea cells exposed to zinc chloride additions
Biotechnol. Bioeng.
102
546-553
2009
Nitrosomonas europaea
brenda
Radniecki, T.S.; Semprini, L.; Dolan, M.E.
Expression of merA, trxA, amoA, and hao in continuously cultured Nitrosomonas europaea cells exposed to cadmium sulfate additions
Biotechnol. Bioeng.
104
1004-1011
2009
Nitrosomonas europaea
brenda
Zeyaullah, M.; Haque, S.; Nabi, G.; Nand, K.; Ali, A.
Molecular cloning and expression of bacterial mercuric reductase gene
Afr. J. Biotechnol.
9
3714-3718
2010
plasmid R100
-
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 (E0XF09)
brenda
Ledwidge, R.; Hong, B.; Doetsch, V.; Miller, S.M.
NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols
Biochemistry
49
8988-8998
2010
Pseudomonas aeruginosa
brenda
Haque, S.; Zeyaullah, M.; Nabi, G.; Srivastava, P.S.; Ali, A.
Transgenic tobacco plant expressing environmental E. coli merA gene for enhanced volatilization of ionic mercury
J. Microbiol. Biotechnol.
20
917-924
2010
Escherichia coli (Q93UN8), Escherichia coli
brenda
Freedman, Z.; Zhu, C.; Barkay, T.
Mercury resistance and mercuric reductase activities and expression among chemotrophic thermophilic Aquificae
Appl. Environ. Microbiol.
78
6568-6575
2012
Hydrogenobaculum sp. Y04AAS1 (B4U9T7), Hydrogenivirga sp. 128-5-R1-1 (A8UT36)
brenda
Zhang, W.; Chen, L.; Liu, D.
Characterization of a marine-isolated mercury-resistant Pseudomonas putida strain SP1 and its potential application in marine mercury reduction
Appl. Microbiol. Biotechnol.
93
1305-1314
2012
Pseudomonas putida, Pseudomonas putida SP1
brenda
Bafana, A.; Chakrabarti, T.; Krishnamurthi, K.
Mercuric reductase activity of multiple heavy metal-resistant Lysinibacillus sphaericus G1
J. Basic Microbiol.
55
285-992
2015
Lysinibacillus sphaericus (D9J041), Lysinibacillus sphaericus, Lysinibacillus sphaericus G1 (D9J041)
brenda
Sayed, A.; Ghazy, M.A.; Ferreira, A.J.; Setubal, J.C.; Chambergo, F.S.; Ouf, A.; Adel, M.; Dawe, A.S.; Archer, J.A.; Bajic, V.B.; Siam, R.; El-Dorry, H.
A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea
J. Biol. Chem.
289
1675-1687
2014
uncultured prokaryote (V5TDP2)
brenda
Johs, A.; Harwood, I.M.; Parks, J.M.; Nauss, R.E.; Smith, J.C.; Liang, L.; Miller, S.M.
Structural characterization of intramolecular Hg2+ transfer between flexibly linked domains of mercuric ion reductase
J. Mol. Biol.
413
639-656
2011
Shigella flexneri
brenda
Lian, P.; Guo, H.B.; Riccardi, D.; Dong, A.; Parks, J.M.; Xu, Q.; Pai, E.F.; Miller, S.M.; Wei, D.Q.; Smith, J.C.; Guo, H.
X-ray structure of a Hg2+ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg2+ transfer between the C-terminal and buried catalytic site cysteine pairs
Biochemistry
53
7211-7222
2014
Pseudomonas aeruginosa
brenda
Bafana, A.; Khan, F.; Suguna, K.
Structural and functional characterization of mercuric reductase from Lysinibacillus sphaericus strain G1
Biometals
30
809-819
2017
Lysinibacillus sphaericus (D9J041), Lysinibacillus sphaericus, Lysinibacillus sphaericus G1 (D9J041)
brenda
Hong, L.; Sharp, M.A.; Poblete, S.; Biehl, R.; Zamponi, M.; Szekely, N.; Appavou, M.S.; Winkler, R.G.; Nauss, R.E.; Johs, A.; Parks, J.M.; Yi, Z.; Cheng, X.; Liang, L.; Ohl, M.; Miller, S.M.; Richter, D.; Gompper, G.; Smith, J.C.
Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase
Biophys. J.
107
393-400
2014
Pseudomonas aeruginosa
brenda
Keirsse-Haquin, J.; Picaud, T.; Bordes, L.; de Gracia, A.G.; Desbois, A.
Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase a resonance Raman study
Eur. Biophys. J.
47
205-223
2018
Cupriavidus metallidurans, Enterococcus faecalis
brenda
Moller, A.K.; Barkay, T.; Hansen, M.; Norman, A.; Hansen, L.; Soslas, S.; rensen, S.; Boyd, E.; Kroer, N.
Mercuric reductase genes (merA) and mercury resistance plasmids in high arctic snow, freshwater and sea-ice brine
FEMS Microbiol. Ecol.
87
52-63
2014
Arthrobacter sp. 8D5s (T1RLC8), Bacillus sp. SOK1b (T1RLH1), Flavobacterium sp. SOK62 (T1RLH3), Pseudomonas sp. SOK13 (T1RLH9), Pseudomonas sp. SOK32 (T1RR74), Pseudomonas sp. SOK33 (T1RRS2), Pseudomonas sp. SOK41 (T1RRM0), Pseudomonas sp. SOK43 (T1RRL9), Pseudomonas sp. SOK44 (T1RLH8), Pseudomonas sp. SOK50 (T1RRS1), Pseudomonas sp. SOK52 (T1RR73), Pseudomonas sp. SOK54 (T1RRJ1), Pseudomonas sp. SOK59 (T1RRJ9), Pseudomonas sp. SOK65 (T1RR77), Pseudomonas sp. SOK68 (T1RRS4), Pseudomonas sp. SOK70 (T1RLC7), Pseudomonas sp. SOK73 (T1RRK2), Pseudomonas sp. SOK75 (T1RRJ7), Pseudomonas sp. SOK80 (T1RR75), Pseudomonas sp. SOK84 (T1RRS3), Pseudomonas sp. SOK85 (T1RRM2), Pseudomonas sp. SOK89 (T1RLH7), Sphingomonas sp. SOK19 (T1RRK0), Sphingomonas sp. SOK19y (T1RRJ3), Sphingomonas sp. SOK5 (T1RRM1), Variovorax sp. SOK15 (T1RLC6)
brenda
Artz, J.H.; White, S.N.; Zadvornyy, O.A.; Fugate, C.J.; Hicks, D.; Gauss, G.H.; Posewitz, M.C.; Boyd, E.S.; Peters, J.W.
Biochemical and structural properties of a thermostable mercuric ion reductase from Metallosphaera sedula
Front. Bioeng. Biotechnol.
3
97
2015
Metallosphaera sedula (A4YG49), Metallosphaera sedula, Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 (A4YG49)
brenda
Giovanella, P.; Cabral, L.; Bento, F.M.; Gianello, C.; Camargo, F.A.
Mercury (II) removal by resistant bacterial isolates and mercuric (II) reductase activity in a new strain of Pseudomonas sp. B50A
New Biotechnol.
33
216-223
2016
Enterobacter sp. A25B, Enterobacter sp. B50C, Pseudomonas entomophila, Pseudomonas entomophila A50A, Pseudomonas entomophila B100A, Pseudomonas putida, Pseudomonas putida V1, Pseudomonas sp. B50A, Pseudomonas sp. B50B, Pseudomonas sp. B50D
brenda
Ramadan, E.; Maged, M.; El Hosseiny, A.; Chambergo, F.S.; Setubal, J.C.; El Dorry, H.
Molecular adaptations of bacterial mercuric reductase to the hypersaline kebrit deep in the Red Sea
Appl. Environ. Microbiol.
85
e01431-18
2019
uncultured bacterium (A0A2H4QUB4)
brenda
Maged, M.; El Hosseiny, A.; Saadeldin, M.K.; Aziz, R.K.; Ramadan, E.
Thermal stability of a mercuric reductase from the Red Sea Atlantis II hot brine environment as analyzed by site-directed mutagenesis
Appl. Environ. Microbiol.
85
e02387-18
2019
uncultured Pseudomonadota bacterium (A0A2H4ZRF8), uncultured Pseudomonadota bacterium
brenda
Krout, I.N.; Scrimale, T.; Vorojeikina, D.; Boyd, E.S.; Rand, M.D.
Organomercurial lyase (MerB)-mediated demethylation decreases bacterial methylmercury resistance in the absence of mercuric reductase (MerA)
Appl. Environ. Microbiol.
88
e0001022
2022
Bacillus cereus, Bacillus cereus RC607
brenda
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