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
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mercury-resistant
- hgcl2
- methylmercury
- lipoamide
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phytoremediation
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mercury-contaminated
- ferrooxidans
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hg-resistant
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geothermal
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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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Substrates Products
Substrates Products on EC 1.16.1.1 - mercury(II) reductase
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REACTION DIAGRAM
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
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?
2,4,6-trinitrobenzenesulfonate + NADPH
? + NADP+
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?
Hg + NADP+ + H+
Hg2+ + NADPH
MerA catalyzes the bioconversion of toxic Hg2+ to the least toxic elemental Hg0, and is capable of reducing the Hg2+, via NADPH as an electron donor
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?
Hg + NADP+ + H+
Hg2+ + NADPH
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Cys11 and Cys14 are involved in metal binding, role for Tyr62 in modulating the pKa values of the cysteine thiols
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?
Hg + NADP+ + H+
Hg2+ + NADPH
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the enzmye reduces reactive Hg2+ to volatile and relatively inert monoatomic Hg0 vapor. Pseudomonas putida SP1 is able to volatilize almost 100% of the total mercury it is exposed to
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r
Hg + NADP+ + H+
Hg2+ + NADPH
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the enzmye reduces reactive Hg2+ to volatile and relatively inert monoatomic Hg0 vapor. Pseudomonas putida SP1 is able to volatilize almost 100% of the total mercury it is exposed to
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r
Hg + NADP+ + H+
Hg2+ + NADPH
organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview
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?
Hg2+ + NADH
Hg + NAD+ + H+
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nearly identical activity with NADPH or NADH
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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last step in bacterial mercury detoxification pathway
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?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense
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mercury resistance is due to the sequential action of two mercury-detoxificating enzymes, organomercurial lyase and mercuric reductase. Enzyme is induced by Hg2+ and organomercurials
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?
Hg2+ + NADPH
Hg + NADP+ + H+
Flavobacterium rigense PR2
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mercury resistance is due to the sequential action of two mercury-detoxificating enzymes, organomercurial lyase and mercuric reductase. Enzyme is induced by Hg2+ and organomercurials
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?
Hg2+ + NADPH
Hg + NADP+ + H+
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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nearly identical activity with NADPH or NADH
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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the enzyme is a key component of an organomercurial detoxification system
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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the enzyme is a key component of an organomercurial detoxification system
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?
Hg2+ + NADPH
Hg + NADP+ + H+
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?
Hg2+ + NADPH
Hg + NADP+ + H+
the merA mutant exhibits mercury sensitivity relative to wild type and is defective in elemental mercury volatilization
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?
Hg2+ + NADPH
Hg(0) + NADP+
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key enzyme in detoxification of mercury in bacteria
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r
Hg2+ + NADPH
Hg(0) + NADP+
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mercuric ion resistance in bacteria requires transport of Hg2+ ions into the cytoplasmic compartment where they are reduced to the less toxic metallic mercury Hg0 by mercuric reductase
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r
Hg2+ + NADPH
Hg(0) + NADP+
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interactions between the inner membrane mercuric ion transporter, MerT, and the N-terminal domain of cytoplasmic mercuric reductase, transport is the rate-limiting step in mercury detoxification, overview
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r
Hg2+ + NADPH
Hg(0) + NADP+
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key enzyme in detoxification of mercury in bacteria
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r
Hg2+ + NADPH
Hg(0) + NADP+
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key enzyme in detoxification of mercury in bacteria
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r
?
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Tyr264 and Tyr605 are involved in substrate binding, Tyr264 is important for catalysis, possibly by destabilizing the binding of Hg(II) to the two ligating thiolates at the active site
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?
additional information
?
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Tyr264 and Tyr605 are involved in substrate binding, Tyr264 is important for catalysis, possibly by destabilizing the binding of Hg(II) to the two ligating thiolates at the active site
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?
additional information
?
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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)
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?
additional information
?
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structure-function study of the N-terminal HMA domain NmerA of Tn501 mercuric ion reductase , i.e. MerA, using NMR and spectral techniques, overview. Determination of NMR solution structures of reduced and Hg2+-bound forms of NmerA
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additional information
?
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Pseudomonas sp. strain B50A exhibiting Mercuric (II) reductase activity removes 86% of the mercury present in the culture medium. ENzyme activity is measured as capacity to remove mercury from the growth medium, activity profile for Pseudomonas sp. B50A, overview
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?
additional information
?
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proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview
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?