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Literature summary for 1.16.1.1 extracted from

  • 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 (2010), Biochemistry, 49, 8988-8998.
    View publication on PubMed
Search for more literature for 1.16.1.1

Protein Variants

Protein Variants Comment Organism
C11A site-directed mutagenesis of NmerA residue of the metal binding site Pseudomonas aeruginosa
C14A site-directed mutagenesis of NmerA residue of the metal binding site Pseudomonas aeruginosa
Y62F site-directed mutagenesis of NmerA residue of the metal binding site Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 2 * 50000, SDS-PAGE Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
 possessing the Tn501 plasmid, a transposon determining resistance to mercuric ions
-

Reaction

Reaction Comment Organism Reaction ID
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 Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg + NADP+ + H+
-
 Pseudomonas aeruginosa Hg2+ + NADPH
-
 ?
Hg + NADP+ + H+ Cys11 and Cys14 are involved in metal binding, role for Tyr62 in modulating the pKa values of the cysteine thiols Pseudomonas aeruginosa Hg2+ + NADPH
-
 ?
additional information 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 aeruginosa ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 50000, SDS-PAGE Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
MerA
-
 Pseudomonas aeruginosa
Tn501 MerA
-
 Pseudomonas aeruginosa
Tn501 mercuric ion reductase
-
 Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
FAD mediates the transfer of electrons betweenNADPH and Hg2+ Pseudomonas aeruginosa
NADPH
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
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 Pseudomonas aeruginosa