Literature summary extracted from
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 (2010), FEMS Microbiol. Lett., 309, 43-47.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.12.1.B1 |
expression in REscherichia coli |
Acidithiobacillus ferrooxidans |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
3.12.1.B1 |
membrane |
outer membrane |
Acidithiobacillus ferrooxidans |
16020 |
- |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.12.1.B1 |
Acidithiobacillus ferrooxidans |
Q0KK37 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.12.1.B1 |
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 |
Acidithiobacillus ferrooxidans |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
3.12.1.B1 |
21 |
- |
recombinant protein, pH 3.0, 30°C |
Acidithiobacillus ferrooxidans |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
3.12.1.B1 |
additional information |
no cofactor required during the refolding process, no cofoactor required for activity |
Acidithiobacillus ferrooxidans |
|