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
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1.16.1.1
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organomercurial
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mercury-resistant
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hgcl2
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methylmercury
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lipoamide
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phytoremediation
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mercury-contaminated
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ferrooxidans
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hg-resistant
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geothermal
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metal-resistant
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phenylmercury
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mercury-polluted
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environmental protection
- 1.16.1.1
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organomercurial
-
mercury-resistant
- hgcl2
- methylmercury
- lipoamide
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phytoremediation
-
mercury-contaminated
- ferrooxidans
-
hg-resistant
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geothermal
-
metal-resistant
- phenylmercury
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mercury-polluted
- environmental protection
Reaction
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
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Subunits
Subunits on EC 1.16.1.1 - mercury(II) reductase
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dimer
homodimer
monomer
trimer
additional information
dimer
Enterobacter sp. A25B
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the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
Enterobacter sp. B50C
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the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
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the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
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the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
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dimer
Pseudomonas entomophila B100A
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the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
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dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
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dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
dimer
-
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA
2 * 60000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
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interfacial active site of the MerA homodimer, structure overview
homodimer
each monomer contributes one active site, made up of a pair of redox-active cysteines, to a catalytic core located at the dimer interface, three-dimensional structure homology modeling, overview
trimer
Yersinia enterolytica 138A14
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3 * 70000, SDS-PAGE
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N-terminal domain NmerA participates in acquisition and delivery of Hg2+ to the catalytic core during thr reduction catalyzed by full-length enzyme
additional information
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N-terminal domain NmerA participates in acquisition and delivery of Hg2+ to the catalytic core during thr reduction catalyzed by full-length enzyme
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additional information
structure comparison of wild-type with mutant Tn501 MerA, PDB ID 1ZK7
additional information
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structure comparison of wild-type with mutant Tn501 MerA, PDB ID 1ZK7
additional information
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
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structure comparison of wild-type with mutant Tn501 MerA, PDB ID 1ZK7
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additional information
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structure comparisons of the mutant C136A/C141A (AACC) Hg2+/NADP+ complex (PDB 4K7Z) and the oxidized wild-type (CCCC) enzyme (PDB 1ZK7)
additional information
Yersinia enterolytica
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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
additional information
Yersinia enterolytica 138A14
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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
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