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Literature summary extracted from

  • 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 (2014), J. Biol. Chem., 289, 1675-1687.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.16.1.1 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 uncultured prokaryote

Protein Variants

EC Number Protein Variants Comment Organism
1.16.1.1 E133G/E134G site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme uncultured prokaryote
1.16.1.1 E15A/E16A site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme uncultured prokaryote
1.16.1.1 E515A/E516A site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme uncultured prokaryote
1.16.1.1 E545A/E546A site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme uncultured prokaryote
1.16.1.1 K432L/P433D/A434L/R435T site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme uncultured prokaryote
1.16.1.1 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 uncultured prokaryote
1.16.1.1 additional information mutations to substitute residues from the ATII-LCL MerA to their corresponding amino acids in the soil enzyme, overview uncultured prokaryote

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.16.1.1 Hg2+ slight inhibition of the ATII-LCL enzyme uncultured prokaryote

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.1.1 additional information
-
 additional information kinetics of wild-type and mutant enzymes, overview uncultured prokaryote

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.16.1.1 additional information the mercuric reductase is functional in high salt and resistant to high concentrations of Hg2+ uncultured prokaryote

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.16.1.1 Hg + NADP+ + H+ uncultured prokaryote
-
 Hg2+ + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.16.1.1 uncultured prokaryote V5TDP2 from the unique deep brine environment of Atlantis II in the Red Sea, lower convective layer, gene merA
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.16.1.1 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 uncultured prokaryote
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.1.1 Hg + NADP+ + H+
-
 uncultured prokaryote Hg2+ + NADPH
-
 r

Subunits

EC Number Subunits Comment Organism
1.16.1.1 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 uncultured prokaryote

Synonyms

EC Number Synonyms Comment Organism
1.16.1.1 mercuric reductase
-
 uncultured prokaryote

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.16.1.1 37
-
 assay at uncultured prokaryote

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.16.1.1 additional information
-
 the mercuric reductase is stable at high temperatures uncultured prokaryote
1.16.1.1 60
-
 10 min, 80% activity remaining uncultured prokaryote
1.16.1.1 75
-
 10 min, 50% inactivation uncultured prokaryote

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.16.1.1 7.4
-
 assay at uncultured prokaryote

Cofactor

EC Number Cofactor Comment Organism Structure
1.16.1.1 FAD
-
 uncultured prokaryote
1.16.1.1 additional information the enzymes contains FAD, utilizes NADPH as an electron donor, and requires an excess of exogenous thiols for activity uncultured prokaryote
1.16.1.1 NADP+
-
 uncultured prokaryote
1.16.1.1 NADPH
-
 uncultured prokaryote

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.16.1.1 0.27
-
 pH 7.4, 37°C uncultured prokaryote Hg2+

General Information

EC Number General Information Comment Organism
1.16.1.1 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 uncultured prokaryote
1.16.1.1 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 uncultured prokaryote