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Literature summary extracted from

  • 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 (2014), Biophys. J., 107, 393-400 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.16.1.1 recombinant expression in Escherichia coli strain BL21(DE3) pLysS Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.16.1.1 Hg2+ + NADPH Pseudomonas aeruginosa
-
 Hg + NADP+ + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.16.1.1 Pseudomonas aeruginosa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.16.1.1 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 Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.1.1 Hg2+ + NADPH
-
 Pseudomonas aeruginosa Hg + NADP+ + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.16.1.1 dimer interdomain dynamics in MerA, overview Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
1.16.1.1 MerA
-
 Pseudomonas aeruginosa
1.16.1.1 mercuric ion reductase
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.16.1.1 FAD
-
 Pseudomonas aeruginosa
1.16.1.1 NADPH
-
 Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.16.1.1 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 Pseudomonas aeruginosa