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1.16.1.1: mercury(II) reductase

This is an abbreviated version!
For detailed information about mercury(II) reductase, go to the full flat file.

Word Map on EC 1.16.1.1

Reaction

Hg
+
NADP+
 +
H+
=
Hg2+
 +
NADPH

Synonyms

bacterial mercuric reductase, Mer A, MerA, MerA protein, mercurate(II) reductase, mercuric (II) reductase, mercuric ion reductase, mercuric reductase, mercury reductase, Msed_1241, MseMerA, reduced NADP:mercuric ion oxidoreductase, reductase, mercurate(II), Rm CH34, Tn501 MerA, Tn501 mercuric ion reductase

ECTree

     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.1 With NAD+ or NADP+ as acceptor
                1.16.1.1 mercury(II) reductase

Engineering

Engineering on EC 1.16.1.1 - mercury(II) reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
Y264F
-
Km-value for Hg2+ is 5fold lower compared to the Km-value of the wild-type enzyme, turn-over number is reduced by 164fold
Y264F/Y605F
-
Km-value for Hg2+ is 5fold lower than the Km-value of the wild-type enzyme, turnover-number is reduced by 1091fold
Y605F
-
Km-value for Hg2+ is 1.3fold higher compared to the Km-value of the wild-type enzyme, turnover-number is reduced by 6.3fold
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
-
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
-
Y264F
-
Km-value for Hg2+ is 5fold lower compared to the Km-value of the wild-type enzyme, turn-over number is reduced by 164fold
-
Y264F/Y605F
-
Km-value for Hg2+ is 5fold lower than the Km-value of the wild-type enzyme, turnover-number is reduced by 1091fold
-
Y605F
-
Km-value for Hg2+ is 1.3fold higher compared to the Km-value of the wild-type enzyme, turnover-number is reduced by 6.3fold
-
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
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
Y605H
-
24fold decrease in turnover number and a 15fold decrease in Km-value
E317V/F441Y
C11A
-
site-directed mutagenesis of NmerA residue of the metal binding site
C136A/C141A
-
site-directed mutagenesis, the C136A/C141A catalytic core mutant. Mutation of either C136 or C141 or both results in a total loss of Hg2+ reductase activity. CRystal structure determination with bound substrates
C14A
-
site-directed mutagenesis of NmerA residue of the metal binding site
Y62F
-
site-directed mutagenesis of NmerA residue of the metal binding site
C135A
-
site-directed mutagenesis
C140A
-
site-directed mutagenesis
C14A
-
site-directed mutagenesis
C561A
-
site-directed mutagenesis
E133G/E134G
site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme
E15A/E16A
site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme
E515A/E516A
site-directed mutagenesis, the mutant shows altered salt and metal resistance and temperature stability compared to the wild-type enzyme
E545A/E546A
site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme
K432L/P433D/A434L/R435T
site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme
K432L/P433D/A434L/R435T/K465D/V466S/G467R/K468T/F469L/P470T
site-directed mutagenesis, the mutant shows salt and metal resistance and temperature stability similar to the wild-type enzyme
additional information