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Literature summary extracted from
- Defects in a quinol oxidase lead to loss of KatC catalase activity in Pseudomonas aeruginosa: KatC activity is temperature dependent and it requires an intact disulphide bond formation system (2006), Biochem. Biophys. Res. Commun., 341, 697-702.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.11.1.6 | additional information | loss of enzyme activity results in a temperature-dependent hydrogen peroxide sensitivity, correlating with its temperature-inducible expression pattern | Pseudomonas aeruginosa |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.11.1.6 | cytoplasm | - |
Pseudomonas aeruginosa | 5737 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.6 | Pseudomonas aeruginosa | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.11.1.6 | additional information | overexpression of cyanide-insensitive terminal oxidase leads to failure to produce temperature-inducible catalyse KatC without affecting transcription of katC. Presence of an intact disulfide bond formation system is required for KatC activity, and enzyme is predicted to contain two cysteine resiudes | Pseudomonas aeruginosa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.11.1.6 | KatC | - |
Pseudomonas aeruginosa |
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Release 2023.1 (January 2023)
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