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Information on EC 1.16.1.1 - mercury(II) reductase
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1.16.1.1 mercury(II) reductaseIUBMB Comments
A dithiol enzyme.
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Word Map
- 1.16.1.1
-
volatilization
-
organomercurial
-
mercury-resistant
- hgcl2
- methylmercury
-
phytoremediation
- lipoamide
- ferrooxidans
-
mercury-contaminated
-
geothermal
-
metal-resistant
- phenylmercury
- environmental protection
The enzyme appears in viruses and cellular organisms
Synonyms
bacterial mercuric reductase, Mer A, MerA, MerA protein, mercurate(II) reductase, mercuric (II) reductase, mercuric ion reductase, mercuric reductase, mercury reductase, Msed_1241, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bacterial mercuric reductase
Mer A
-
-
-
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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
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-
mercuric reductase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hg + NADP+ + H+ = Hg2+ + NADPH
-
-
-
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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
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Hg + NADP+ + H+ = Hg2+ + NADPH
catalytic mechanisms of the flavoprotein MerA, overview
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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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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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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
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
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
-
-
-
?
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
-
-
-
?
Hg + NADP+ + H+
Hg2+ + NADPH
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
-
-
?
Hg + NADP+ + H+
Hg2+ + NADPH
-
Cys11 and Cys14 are involved in metal binding, role for Tyr62 in modulating the pKa values of the cysteine thiols
-
-
?
Hg + NADP+ + H+
Hg2+ + NADPH
-
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
-
-
r
Hg + NADP+ + H+
Hg2+ + NADPH
-
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
-
-
r
Hg + NADP+ + H+
Hg2+ + NADPH
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
-
-
?
Hg2+ + NADH
Hg + NAD+ + H+
-
nearly identical activity with NADPH or NADH
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
-
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
-
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
-
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
last step in bacterial mercury detoxification pathway
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense
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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
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense PR2
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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
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
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nearly identical activity with NADPH or NADH
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
the enzyme is a key component of an organomercurial detoxification system
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-
?
Hg2+ + NADPH
Hg + NADP+ + H+
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the enzyme is a key component of an organomercurial detoxification system
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
-
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
the merA mutant exhibits mercury sensitivity relative to wild type and is defective in elemental mercury volatilization
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-
?
Hg2+ + NADPH
Hg(0) + NADP+
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key enzyme in detoxification of mercury in bacteria
-
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r
Hg2+ + NADPH
Hg(0) + NADP+
-
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
-
-
r
Hg2+ + NADPH
Hg(0) + NADP+
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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
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-
r
Hg2+ + NADPH
Hg(0) + NADP+
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key enzyme in detoxification of mercury in bacteria
-
-
r
Hg2+ + NADPH
Hg(0) + NADP+
-
key enzyme in detoxification of mercury in bacteria
-
-
r
additional information
?
-
-
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
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-
?
additional information
?
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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
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?
additional information
?
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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)
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?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
-
proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview
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-
?
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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
Hg + NADP+ + H+
Hg2+ + NADPH
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
-
-
?
Hg + NADP+ + H+
Hg2+ + NADPH
-
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
-
-
r
Hg + NADP+ + H+
Hg2+ + NADPH
-
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
-
-
r
Hg + NADP+ + H+
Hg2+ + NADPH
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
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
last step in bacterial mercury detoxification pathway
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense
-
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
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense PR2
-
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
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
-
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
the enzyme is a key component of an organomercurial detoxification system
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
-
the enzyme is a key component of an organomercurial detoxification system
-
-
?
Hg2+ + NADPH
Hg + NADP+ + H+
the merA mutant exhibits mercury sensitivity relative to wild type and is defective in elemental mercury volatilization
-
-
?
Hg2+ + NADPH
Hg(0) + NADP+
-
key enzyme in detoxification of mercury in bacteria
-
-
r
Hg2+ + NADPH
Hg(0) + NADP+
-
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
-
-
r
Hg2+ + NADPH
Hg(0) + NADP+
-
key enzyme in detoxification of mercury in bacteria
-
-
r
Hg2+ + NADPH
Hg(0) + NADP+
-
key enzyme in detoxification of mercury in bacteria
-
-
r
additional information
?
-
-
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
-
-
?
additional information
?
-
proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
a flavoprotein, spectral analysis of the binding structure and environment, overview
NADPH
-
-
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
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
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
0.035
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
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady-state kinetic analysis, overview, apparent second-order rate constant for Hg(II) transfer from MerB to NmerA
-
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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
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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
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
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
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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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
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
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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
MerA catalyzes the bioconversion of toxic Hg2+ to the least toxic elemental Hg0
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
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
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
-
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
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
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
-
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
-
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
-
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
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 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
-
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
-
Show AA Sequence and Transmembrane Helices (6177 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
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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
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
80
97
purified recombinant His-tagged enzyme, pH 6.7, 100 min, activity remaining
additional information
the mercuric reductase is stable at high temperatures
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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
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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