BRENDA - Enzyme Database
show all sequences of 1.8.5.5

Thiosulfate reduction in Salmonella enterica is driven by the proton motive force

Stoffels, L.; Krehenbrink, M.; Berks, B.C.; Unden, G.; J. Bacteriol. 194, 475-485 (2012)

Data extracted from this reference:

Organism
Organism
UniProt
Commentary
Textmining
Salmonella enterica
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Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
sulfite + hydrogen sulfide + menaquinone
-
725273
Salmonella enterica
thiosulfate + menaquinol
thiosulfate reductase is able to catalyze the combined oxidation of sulfide and sulfite to thiosulfate in a reverse of the physiological reaction
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r
thiosulfate + menaquinol
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725273
Salmonella enterica
sulfite + hydrogen sulfide + menaquinone
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r
Cofactor
Cofactor
Commentary
Organism
Structure
menaquinol
menaquinol is the sole electron donor to thiosulfate reductase
Salmonella enterica
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
menaquinol
menaquinol is the sole electron donor to thiosulfate reductase
Salmonella enterica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
sulfite + hydrogen sulfide + menaquinone
-
725273
Salmonella enterica
thiosulfate + menaquinol
thiosulfate reductase is able to catalyze the combined oxidation of sulfide and sulfite to thiosulfate in a reverse of the physiological reaction
-
-
r
thiosulfate + menaquinol
-
725273
Salmonella enterica
sulfite + hydrogen sulfide + menaquinone
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-
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r
General Information
General Information
Commentary
Organism
physiological function
thiosulfate reductase activity depends on the proton motive force across the cytoplasmic membrane. The proton motive force drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase is able to catalyze the combined oxidation of sulfide and sulfite to thiosulfate in a reverse of the physiological reaction. In contrast to the forward reaction, the exergonic thiosulfate-forming reaction is independent of the proton motive force
Salmonella enterica
General Information (protein specific)
General Information
Commentary
Organism
physiological function
thiosulfate reductase activity depends on the proton motive force across the cytoplasmic membrane. The proton motive force drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase is able to catalyze the combined oxidation of sulfide and sulfite to thiosulfate in a reverse of the physiological reaction. In contrast to the forward reaction, the exergonic thiosulfate-forming reaction is independent of the proton motive force
Salmonella enterica
Other publictions for EC 1.8.5.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
725273
Stoffels
Thiosulfate reduction in Salmo ...
Salmonella enterica
J. Bacteriol.
194
475-485
2012
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1
1
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645578
Bang
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Cadmium, lead, and zinc remova ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biotechnol. Lett.
22
1331-1335
2000
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1
1
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737488
Bang
Engineering hydrogen sulfide p ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
Appl. Environ. Microbiol.
66
3939-3944
2000
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1
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7
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738317
Alami
Cloning and characterization o ...
Salmonella enterica subsp. enterica serovar Typhimurium
Gene
156
53-57
1995
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6
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1
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738502
Heinzinger
Sequence analysis of the phs o ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
J. Bacteriol.
177
2813-2820
1995
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3
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6
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738491
Clark
The phs gene and hydrogen sulf ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
169
2391-2397
1987
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