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Information on EC 1.16.1.1 - mercury(II) reductase and Organism(s) Metallosphaera sedula and UniProt Accession A4YG49
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1.16.1.1 mercury(II) reductaseIUBMB Comments
A dithiol enzyme.
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Word Map
- 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
The taxonomic range for the selected organisms is: Metallosphaera sedula
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mercuric reductase, mercuric ion reductase, mercury reductase, mer a, bacterial mercuric reductase, mera protein, tn501 mera, mercuric (ii) reductase, mercury(ii) reductase, tn501 mercuric ion reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mer A
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mercurate(II) reductase
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mercuric ion reductase
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mercuric reductase
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mercury reductase
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reduced NADP:mercuric ion oxidoreductase
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reductase, mercurate(II)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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SYSTEMATIC NAME
IUBMB Comments
Hg:NADP+ oxidoreductase
A dithiol enzyme.
CAS REGISTRY NUMBER
COMMENTARY
67880-93-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.9
NADPH oxidation-linked Hg2+ reduction specific activity, purified recombinant His-tagged enzyme, pH 6.7, 37°C
3.1
NADPH oxidation-linked Hg2+ reduction specific activity, purified recombinant His-tagged enzyme, pH 6.7, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 70
assay at, enzyme activity at 70°C is about 1.6fold higher compared to activity at 37°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
Metallosphaera sedula is isolated from Pisciarelli Solfatara in Naples, Italy. Pisciarelli Solfatara contains a variety of thermal features that range in temperature from about 30°C to nearly 100°C, and a pH range of pH 1.5 to around pH 6.0 with elevated concentrations of heavy metals, including Hg2+ at concentrations up to 0.005g/kg
additional information
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Metallosphaera sedula is isolated from Pisciarelli Solfatara in Naples, Italy. Pisciarelli Solfatara contains a variety of thermal features that range in temperature from about 30°C to nearly 100°C, and a pH range of pH 1.5 to around pH 6.0 with elevated concentrations of heavy metals, including Hg2+ at concentrations up to 0.005g/kg
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
MerA is part of the disulfide oxidoreductase (DSOR) family, are ancient enzymes that have arisen in high temperature environments after the great oxidation event about 2.4 billion years ago
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinanat His-tagged enzyme, vapour diffusion hanging drop method, from 0.085 M Tris, pH 8.5, 15% v/v glycerol, 14% w/v PEG 400, 0.19 M LiSO4, and 20 mg/ml protein, 2 weeks, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement using Tn501 MerA, PDB ID 1ZK7, as template, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E317V/F441Y
mutant Tn501 MerA, structure comparison with the wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
97
purified recombinant His-tagged enzyme, pH 6.7, 100 min, activity remaining
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Msed_1241, phylogenetic analysis and tree, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Artz, J.H.; White, S.N.; Zadvornyy, O.A.; Fugate, C.J.; Hicks, D.; Gauss, G.H.; Posewitz, M.C.; Boyd, E.S.; Peters, J.W.
Biochemical and structural properties of a thermostable mercuric ion reductase from Metallosphaera sedula
Front. Bioeng. Biotechnol.
3
97
2015
Metallosphaera sedula (A4YG49), Metallosphaera sedula, Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 (A4YG49)
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