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Literature summary for 1.16.1.1 extracted from

  • Moore, M.J.; Miller, S.M.; Walsh, C.T.
    C-Terminal cysteines of Tn501 mercuric ion reductase (1992), Biochemistry, 31, 1677-1685.
    View publication on PubMed
Search for more literature for 1.16.1.1

Protein Variants

Protein Variants Comment Organism
C558A mutation results in a total disruption of the Hg(II) detoxification pathway in vivo, compared to wild-type enzyme the mutant shows a 20fold reduction in turnover number and a 10fold increase in Km Escherichia coli
C559A mutation results in a total disruption of the Hg(II) detoxification pathway in vivo, compared to wild-type enzyme less than a 2fold reduction in turnover number and an increase in Km-value of 4-5fold Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
 Hg2+ wild-type enzyme, aerobic conditions Escherichia coli
0.0057
-
 Hg2+ wild-type enzyme, anaerobic conditions Escherichia coli
0.021
-
 Hg2+ mutant enzyme C559A, anaerobic conditions Escherichia coli
0.025
-
 Hg2+ mutant enzyme C559A, aerobic conditions Escherichia coli
0.045
-
 Hg2+ mutant enzyme C558A, aerobic conditions Escherichia coli
0.052
-
 Hg2+ mutant enzyme C558A, anaerobic conditions Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hg2+ + NADPH Escherichia coli last step in bacterial mercury detoxification pathway Hg + NADP+ + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 Tn501 mercuric ion reductase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg2+ + NADPH
-
 Escherichia coli Hg + NADP+ + H+
-
 ?
Hg2+ + NADPH last step in bacterial mercury detoxification pathway Escherichia coli Hg + NADP+ + H+
-
 ?
additional information Cys558 plays a more important role in forming the reducible complex with Hg(II), while both Cys558 and Cys559 seem to be involved in efficient scavenging of Hg(II) Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.383
-
 Hg2+ mutant enzyme C558A, anaerobic conditions Escherichia coli
0.5
-
 Hg2+ mutant enzyme C558A, aerobic conditions Escherichia coli
4.85
-
 Hg2+ mutant enzyme C559A, anaerobic conditions Escherichia coli
7.43
-
 Hg2+ wild-type enzyme, aerobic conditions Escherichia coli
7.63
-
 Hg2+ mutant enzyme C559A, aerobic conditions Escherichia coli
13.5
-
 Hg2+ wild-type enzyme, aerobic conditions Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Escherichia coli