EC Number   |
General Information |
Reference |
|---|
   3.12.1.B1 | 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 |
734092 |
| 3.12.1.B1 | metabolism |
the enzyme is a key enzyme in the dissimilatory sulfur oxidation pathway in this bacterium |
733533 |
| 3.12.1.B1 | metabolism |
the enzyme is involved in tetrathionate metabolism, but also in thiosulfate and elemental sulfur metabolism |
-, 756219 |
| 3.12.1.B1 | 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 |
734092 |
| 3.12.1.B1 | more |
the sole cysteine residue, Cys301, of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does neither play a role in enzyme activity nor in subunit assembly |
733533 |
| 3.12.1.B1 | physiological function |
the enzyme is a key enzyme in hydrolysis of tetrathionate for usage as sole energy source |
734092 |
| 3.12.1.B1 | physiological function |
the enzyme is key enzyme in the dissimilatory sulfur oxidation pathway and catalyzes tetrathionate hydrolysis to generate elemental sulfur, thiosulfate, and sulfate |
733533 |
| 3.12.1.B1 | 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 |
725078 |
