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pentathionate + H2O
2 sulfur + thiosulfate + sulfate + 2 H+
tetrathionate + H2O
pentathionate + thiosulfate + sulfate
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
tetrathionate + H2O
thiosulfate + sulfate + sulfur + 2 H+
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-
-
?
additional information
?
-
pentathionate + H2O
2 sulfur + thiosulfate + sulfate + 2 H+
-
-
-
-
?
pentathionate + H2O
2 sulfur + thiosulfate + sulfate + 2 H+
-
80% of the activity with tetrathionate
-
-
?
tetrathionate + H2O
pentathionate + thiosulfate + sulfate
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no detection of elemental sulfur
-
?
tetrathionate + H2O
pentathionate + thiosulfate + sulfate
-
no detection of elemental sulfur
-
?
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
-
-
-
?
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
-
-
-
-
?
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
-
-
stoichiometric conversion of tetrathionate to thiosulfate, sulfur and two protons
-
?
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
Q0KK37
-
-
-
?
tetrathionate + H2O
sulfur + thiosulfate + sulfate + 2 H+
-
the end products of hydrolysis of both tetrathionate and pentathionate by the pure enzyme are thiosulfate, sulfur and sulfate
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-
?
additional information
?
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-
hydrolysis of trithionate, reaction of EC 3.12.1.1, and of tetrathionate are catalyzed by two different enzymes
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-
?
additional information
?
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enzyme additionally shows Fe3+-reductase activity, catalyzing Fe3+ reduction with tetrathionate. Tetrathionate hydrolase produces Fe2+ from with tetrathionate during growth on tetrathionate
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-
?
additional information
?
-
-
enzyme additionally shows Fe3+-reductase activity, catalyzing Fe3+ reduction with tetrathionate. Tetrathionate hydrolase produces Fe2+ from with tetrathionate during growth on tetrathionate
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-
?
additional information
?
-
-
no substrates: trithionate, hexathionate
-
-
?
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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
the enzyme is a key enzyme in the dissimilatory sulfur oxidation pathway in this bacterium
metabolism
the organism can obtain energy from the oxidation of Fe2+, H2, and sulfur, and various reduced inorganic sulfur compounds (RISCs). Tetrathionate is a key intermediate during RISC oxidation, hydrolyzed by tetrathionate hydrolase (TetH), and used as sole energy source. Genes tetH and doxD2 act synergistically, and doxD2 is considered important in thiosulfate metabolism
metabolism
-
the enzyme is involved in tetrathionate metabolism, but also in thiosulfate and elemental sulfur metabolism
metabolism
-
the enzyme is involved in tetrathionate metabolism, but also in thiosulfate and elemental sulfur metabolism
-
physiological function
under oxygen-sufficient conditions strain oxidizes thiosulfate to tetrathionate, which accumulates in the culture medium. Tetrathionate is then oxidized by tetrathionate hydrolase generating thiosulfate, elemental sulfur, and sulfate as final products. In thiosulfate-grown cultures shifted to oxygen-limiting conditions a massive production of extracellular conspicuous sulfur globules is seen, with concomitant decrease in tetrathionate concentration. Cellular tetrathionate hydrolase activity is negligible in oxygen-limiting conditions, while extracellular activity is high under both conditions
physiological function
the enzyme is a key enzyme in hydrolysis of tetrathionate for usage as sole energy source
physiological function
the enzyme is key enzyme in the dissimilatory sulfur oxidation pathway and catalyzes tetrathionate hydrolysis to generate elemental sulfur, thiosulfate, and sulfate
additional information
the sole cysteine residue, Cys301, of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does neither play a role in enzyme activity nor in subunit assembly
additional information
-
the sole cysteine residue, Cys301, of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does neither play a role in enzyme activity nor in subunit assembly
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monomer
and dimer, 1 * 54000, SDS-PAGE, x * 53642, calculated without gylcosylation
?
x * 55000, dimers and multimers, SDS-PAGE
?
-
x * 55000, dimers and multimers, SDS-PAGE
-
dimer
and monomer, 2 * 54000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
2 * 52000, SDS-PAGE and MALDI-TOF
dimer
-
2 * 52000, SDS-PAGE and MALDI-TOF
-
homodimer
-
homodimer
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2 * 52000, SDS-PAGE
homodimer
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2 * 52000, SDS-PAGE
-
additional information
-
the enzyme produces filamentous particles with a zipper-like appearance that represent a secreted form of a the genuine cellular enzyme, tetrathionate hydrolase. The purified zipper-like proteins appear as cylindrical particles uniform in their width, 15 nm, and variable in length, 100 to 200 nm
additional information
the enzyme produces filamentous particles with a zipper-like appearance that represent a secreted form of a the genuine cellular enzyme, tetrathionate hydrolase. The purified zipper-like proteins appear as cylindrical particles uniform in their width, 15 nm, and variable in length, 100 to 200 nm
additional information
-
the enzyme produces filamentous particles with a zipper-like appearance that represent a secreted form of a the genuine cellular enzyme, tetrathionate hydrolase. The purified zipper-like proteins appear as cylindrical particles uniform in their width, 15 nm, and variable in length, 100 to 200 nm
-
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Kanao, T.; Kosaka, M.; Yoshida, K.; Nakayama, H.; Tamada, T.; Kuroki, R.; Yamada, H.; Takada, J.; Kamimura, K.
Crystallization and preliminary X-ray diffraction analysis of tetrathionate hydrolase from Acidithiobacillus ferrooxidans
Acta Crystallogr. Sect. F
69
692-694
2013
Acidithiobacillus ferrooxidans (Q0KK37), Acidithiobacillus ferrooxidans
brenda
Krupovic, M.; Peixeiro, N.; Bettstetter, M.; Rachel, R.; Prangishvili, D.
Archaeal tetrathionate hydrolase goes viral: secretion of a sulfur metabolism enzyme in the form of virus-like particles
Appl. Environ. Microbiol.
78
5463-5465
2012
Acidianus hospitalis, Acidianus hospitalis (F4B6C8), Acidianus hospitalis YS8, Acidianus hospitalis W1 (F4B6C8)
brenda
Sugio, T.; Taha, T.M.; Takeuchi, F.
Ferrous iron production mediated by tetrathionate hydrolase in tetrathionate-, sulfur-, and iron-grown Acidithiobacillus ferrooxidans ATCC 23270 cells
Biosci. Biotechnol. Biochem.
73
1381-1386
2009
Acidithiobacillus ferrooxidans (B7J3C9), Acidithiobacillus ferrooxidans
brenda
De Jong, G.A.H.; Hazeu, W.; Bos, P.; Kuenen, J.G.
Isolation of the tetrathionate hydrolase from Thiobacillus acidophilus
Eur. J. Biochem.
243
678-683
1997
Acidiphilium acidophilum
brenda
Bugaytsova, Z.; Lindstrom, E.B.
Localization, purification and properties of a tetrathionate hydrolase from Acidithiobacillus caldus
Eur. J. Biochem.
271
272-280
2004
Acidithiobacillus caldus (A4ZV25), Acidithiobacillus caldus, Acidithiobacillus caldus DSM 8584 (A4ZV25)
brenda
Meulenberg, R.; Scheer, E.J.; Pronk, J.T.; Hazeu, W.; Bos, P.; Kuenen, J.G.
Metabolism of tetrathionate in Thiobacillus acidophilus
FEMS Microbiol. Lett.
112
167-172
1993
Acidiphilium acidophilum
-
brenda
Kanao, T.; Matsumoto, C.; Shiraga, K.; Yoshida, K.; Takada, J.; Kamimura, K.
Recombinant tetrathionate hydrolase from Acidithiobacillus ferrooxidans requires exposure to acidic conditions for proper folding
FEMS Microbiol. Lett.
309
43-47
2010
Acidithiobacillus ferrooxidans (Q0KK37), Acidithiobacillus ferrooxidans
brenda
Protze, J.; Mueller, F.; Lauber, K.; Nab, B.; Mentele, R.; Lottspeich, F.; Kletzin, A.
An extracellular tetrathionate hydrolase from the thermoacidophilic archaeon Acidianus ambivalens with an activity optimum at pH 1
Front. Microbiol.
2
68
2011
Acidianus ambivalens (G8YXZ9), Acidianus ambivalens
brenda
Beard, S.; Paradela, A.; Albar, J.P.; Jerez, C.A.
Growth of Acidithiobacillus ferrooxidans ATCC 23270 in thiosulfate under oxygen-limiting conditions generates extracellular sulfur globules by means of a secreted tetrathionate hydrolase
Front. Microbiol.
2
79
2011
Acidithiobacillus ferrooxidans (B7J3C9), Acidithiobacillus ferrooxidans
brenda
De Jong, G.A.H.; Hazeu, W.; Bos, P.; Kuenen, J.G.
Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans
Microbiology
143
499-504
1997
Acidithiobacillus ferrooxidans
brenda
Kanao, T.; Nakayama, H.; Kato, M.; Kamimura, K.
The sole cysteine residue (Cys301) of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does not play a role in enzyme activity
Biosci. Biotechnol. Biochem.
78
2030-2035
2014
Acidithiobacillus ferrooxidans (B7J3C9), Acidithiobacillus ferrooxidans
brenda
Yu, Y.; Liu, X.; Wang, H.; Li, X.; Lin, J.
Construction and characterization of tetH overexpression and knockout strains of Acidithiobacillus ferrooxidans
J. Bacteriol.
196
2255-2264
2014
Acidithiobacillus ferrooxidans (B7J3C9), Acidithiobacillus ferrooxidans
brenda
Kanao, T.; Onishi, M.; Kajitani, Y.; Hashimoto, Y.; Toge, T.; Kikukawa, H.; Kamimura, K.
Characterization of tetrathionate hydrolase from the marine acidophilic sulfur-oxidizing bacterium, Acidithiobacillus thiooxidans strain SH
Biosci. Biotechnol. Biochem.
82
152-160
2018
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans SH
brenda
Wang, Z.B.; Li, Y.Q.; Lin, J.Q.; Pang, X.; Liu, X.M.; Liu, B.Q.; Wang, R.; Zhang, C.J.; Wu, Y.; Lin, J.Q.; Chen, L.X.
The two-component system RsrS-RsrR regulates the tetrathionate intermediate pathway for thiosulfate oxidation in Acidithiobacillus caldus
Front. Microbiol.
7
1755
2016
Acidithiobacillus caldus, Acidithiobacillus caldus MTH-04
brenda
Othman, E.; Yusof, F.; Azmi, A.
Application of plackett-burman design for screening of parameters for the production of tetrathionate hydrolase by Thiobacillus ferrooxidans
J. Eng. Sci. Technol.
10
12-21
2015
Acidithiobacillus ferrooxidans
-
brenda