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Literature summary for 1.16.1.1 extracted from

  • Engst, S.; Miller, S.M.
    Alternative Routes for Entry of HgX2 into the Active Site of Mercuric Ion Reductase Depend on the Nature of the X Ligands (1999), Biochemistry, 38, 3519-3529.
    View publication on PubMed
Search for more literature for 1.16.1.1

Protein Variants

Protein Variants Comment Organism
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 Bacillus sp. (in: Bacteria)
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 Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) RC607
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg2+ + NADPH
-
 Bacillus sp. (in: Bacteria) Hg + NADP+ + H+
-
 ?
Hg2+ + NADPH
-
 Bacillus sp. (in: Bacteria) RC607 Hg + NADP+ + H+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Bacillus sp. (in: Bacteria)