bacterial mercuric reductase, Mer A, MerA, MerA protein, mercurate(II) reductase, mercuric (II) reductase, mercuric ion reductase, mercuric reductase, mercury reductase, Msed_1241, more
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
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
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
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
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
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
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
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
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
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
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
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
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)
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
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
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
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
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
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
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
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
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
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
marine-isolated mercury-resistant strain, isolated from seawater collected from Yantai coastal zone in Shandong Province, China, gene merA encoded in the mer operon
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
enzyme encoded by Tn5044 merA gene, thermosensitive resistance to mercury, expression and functional activity of enzyme are severely inhibited at 37-41.5°C
marine-isolated mercury-resistant strain, isolated from seawater collected from Yantai coastal zone in Shandong Province, China, gene merA encoded in the mer operon
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
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
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
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
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
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
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
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
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
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
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
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
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
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
comparison of structural changes upon metal binding in normally appended metal binding proteins: NmerA with and without Hg2+ , PDB entry 2KT3 and 2KT2, respectively
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
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
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
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
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
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
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 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 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 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 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 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 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 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
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 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 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 enzyme shows extensive sequence homology and functional similarities in the active site of mercuric reductase and nicotinamide disulfide oxidoreductase
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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