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Literature summary for 1.16.1.1 extracted from

  • Blaghen, M.; Vidon, D.J.M.; El Kebbaj, M.S.
    Purification and properties of mercuric reductase from Yersinia enterocolitica 138A14 (1993), Can. J. Microbiol., 39, 193-200.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol required for activity with merthiolate Yersinia enterolytica

Inhibitors

Inhibitors Comment Organism Structure
Ag2+
-
Yersinia enterolytica
Cd2+ weak inhibition Yersinia enterolytica
Cu2+
-
Yersinia enterolytica
HgCl2 activity is inhibited by an excess of HgCl2 Yersinia enterolytica
Mn2+ weak inhibition Yersinia enterolytica
Ni2+
-
Yersinia enterolytica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the Km-value for HgCl2 is dependent on the concentration of exogenous thiol compounds Yersinia enterolytica
0.2
-
Hg 20 mM 2-mercaptoethanol Yersinia enterolytica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
3 * 70000, SDS-PAGE Yersinia enterolytica
200000
-
gel filtration Yersinia enterolytica

Organism

Organism UniProt Comment Textmining
Yersinia enterolytica
-
138A14
-
Yersinia enterolytica 138A14
-
138A14
-

Purification (Commentary)

Purification (Comment) Organism
-
Yersinia enterolytica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.08
-
-
Yersinia enterolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg + NADP+ + H+
-
Yersinia enterolytica Hg2+ + NADPH
-
r
Hg + NADP+ + H+
-
Yersinia enterolytica 138A14 Hg2+ + NADPH
-
r
Hg2+ + NADPH
-
Yersinia enterolytica Hg + NADP+ + H+
-
?
Hg2+ + NADPH
-
Yersinia enterolytica 138A14 Hg + NADP+ + H+
-
?
merthiolate + NADPH
-
Yersinia enterolytica ? + NADP+
-
?
merthiolate + NADPH
-
Yersinia enterolytica 138A14 ? + NADP+
-
?

Subunits

Subunits Comment Organism
More 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 Yersinia enterolytica
trimer 3 * 70000, SDS-PAGE Yersinia enterolytica

Cofactor

Cofactor Comment Organism Structure
FAD contains FAD Yersinia enterolytica
NADPH
-
Yersinia enterolytica

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.016
-
Ag2+
-
Yersinia enterolytica
0.0175
-
Ni2+
-
Yersinia enterolytica
0.018
-
Cu2+
-
Yersinia enterolytica