Literature summary for 3.12.1.B1 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in REscherichia coli	Acidithiobacillus ferrooxidans

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	outer membrane	Acidithiobacillus ferrooxidans	16020	-

Organism

Organism	UniProt	Comment	Textmining
Acidithiobacillus ferrooxidans	Q0KK37	-	-

Purification (Commentary)

Purification (Comment)	Organism
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]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
21	-	recombinant protein, pH 3.0, 30°C	Acidithiobacillus ferrooxidans

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no cofactor required during the refolding process, no cofoactor required for activity	Acidithiobacillus ferrooxidans

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Release 2023.1 (January 2023)