Information on EC 3.12.1.B1 - tetrathionate hydrolase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.12.1.B1
preliminary BRENDA-suppplied EC number
RECOMMENDED NAME
GeneOntology No.
tetrathionate hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tetrathionate + H2O = thiosulfate + sulfate + sulfur + 2 H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
tetrathionate thiosulfohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
188364-81-0
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the DELTAtetH mutant can survive in ferrous medium with an Fe2+ oxidation rate similar to that of the wild-type. For the tetH overexpression strain, the rate is relatively higher than that of the wild type
metabolism
physiological function
additional information
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the sole cysteine residue, Cys301, of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does neither play a role in enzyme activity nor in subunit assembly
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pentathionate + H2O
2 sulfur + thiosulfate + sulfate + 2 H+
show the reaction diagram
tetrathionate + H2O
pentathionate + thiosulfate + sulfate
show the reaction diagram
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
show the reaction diagram
tetrathionate + H2O
thiosulfate + sulfate + sulfur + 2 H+
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
1 mM, more than 10fold stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HgCl2
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0.05 mM, complete loss of activity
thiosulfate
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product inhibition, 40% inhibition at 1 mM
additional information
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not inhibitory: azide at 1 mM, N-ethylmaleimide at 0.05 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium sulfate
sulfate
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strong stimulation, maximal activity between 1 M and 2 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.8
tetrathionate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
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recombinant protein, pH 3.0, 30C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
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no residual activity
2
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about 50% of maximum activity
6
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no residual activity
7
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no residual activity
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
modest activity
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.8
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
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2 * 48000, SDS-PAGE
52000
2 * 52000, SDS-PAGE and MALDI-TOF
52300
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x * 52300, SDS-PAGE
53642
and dimer, 1 * 54000, SDS-PAGE, x * 53642, calculated without gylcosylation
54000
gel filtration
55000
x * 55000, dimers and multimers, SDS-PAGE
93000
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recombinant wild-type enzyme, gel filtration
100000
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gel filtration
105000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
and dimer, 1 * 54000, SDS-PAGE, x * 53642, calculated without gylcosylation
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
N-terminal amino acid sequence Gly-Pro-Ile-Val-Tyr-Thr-Tyr-Thr-Glu-Tyr-Asn-Gly-Thr-Tyr with Asn being glycosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structural model of enzyme shows an eight-bladed beta-propeller topology. The electrostatic surface charge distribution reveals an overall opposite charge on the two faces of the discshaped molecule
to 2.15 A resolution, space group P31 or P32, with unit-cell parameters a = b = 92.1, c = 232.6 A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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100 h, complete loss of activity
40
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20 h, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, enzyme is not affected by freezing and thawing
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0C, stable for one week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli results in the formation of inclusion bodies of the protein in an inactive form. The recombinant protein can be successfully activated after an in vitro refolding treatment. The enzyme requires exposure to an acidicenvironment during protein folding for activation
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high salt concentrations are needed to release enzyme activity during cell disruption
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recombinant inactive wild-type and mutant enzymes refolded from Escherichia coli strain BL21 Star(DE3) inclusion bodies
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21 Star(DE3) in inclusion bodies in an inactive form
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expression in Escherichia coli
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expression in REscherichia coli
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gene tetH, genes tetH and doxD2 act synergistically, and doxD2 is considered important in thiosulfate metabolism, quantitative reverse transcription-PCR analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C301A
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site-directed mutagenesis, the enzyme activities measured in the cysteine-deficient and wild-type enzymes are the same
additional information
construction of a tetH knockout mutant DELTAtetH and a tetH overexpression strain, the tetH overexpression strain grows better on sulfur and tetrathionate and possesses a higher rate of tetrathionate utilization and TetH activity than the wild-type. The DELTAtetH mutant cannot grow on tetrathionate but can proliferate on sulfur with a lower cell yield than the wild type
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding of recombinant inactive wild-type and mutant enzymes from Escherichia coli strain BL21 Star(DE3) inclusion bodies
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis