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Literature summary for 3.4.24.B20 extracted from
- FtsH cleavage of non-native conformations of proteins (2010), J. Struct. Biol., 171, 117-124.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type enzyme in Escherichia coli strain AR5771 | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Escherichia coli | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli |  |
| Zn2+ | required | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Anabaena apoflavodoxin + H2O | Escherichia coli | FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview | ? | - |
? | |
| additional information | Escherichia coli | fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | FtsH is subject to selfprocessing and removes its C-terminal 7 amino acid residues | Escherichia coli |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type enzyme from Escherichia coli strain AR5771 | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Anabaena apoflavodoxin + H2O | FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview | Escherichia coli | ? | - |
? | |
| Anabaena apoflavodoxin + H2O | FtsH degradation of 31 point mutants of Anabaena apoflavodoxin from Anabaena PCC 7119 is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form | Escherichia coli | ? | - |
? | |
| additional information | fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FtsH | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 42 | - |
- |
Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | FtsH is a peculiar prokaryotic protease with low unfoldase activity. FtsH takes care of degrading unstable or inappropriately assembled proteins | Escherichia coli |
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Release 2023.1 (January 2023)
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