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Literature summary for 3.4.24.B17 extracted from
- Conserved pore residues in the AAA protease, FtsH, are important for proteolysis and its coupling to ATP hydrolysis (2003), J. Biol. Chem., 278, 50182-50187.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | unfolded or uncomplexed protein substrates, protein sigma32 and casein, stimulate 1 to 2fold the wild-type enzyme and the mutants F228K, F228E, and F228A, but not G230A | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutants | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F228A | site-directed point mutation, proteolytically inactive with protein sigma32, but degrades casein, decreased ATPase activity | Escherichia coli |
| F228E | site-directed point mutation, proteolytically inactive mutant, increased ATPase activity | Escherichia coli |
| F228K | site-directed point mutation, proteolytically inactive mutant, highly decreased ATPase activity | Escherichia coli |
| G230A | site-directed point mutation, proteolytically inactive mutant, highly decreased ATPase activity | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | integral, active site facing the cytoplasm | Escherichia coli | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protein + H2O | Escherichia coli | - |
peptides | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutants | Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| proteolytic degradation of proteins | enzyme is a AAA protease, highly conserved residues Phe228 and Gly230 lie in the central pore region of the hexamer and are important in proteolysis and coupling to ATP | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.113 | - |
purified recombinant mutant G230A | Escherichia coli |
| 0.122 | - |
purified recombinant mutant F228K | Escherichia coli |
| 0.349 | - |
purified recombinant mutant F228A | Escherichia coli |
| 0.735 | - |
purified recombinant wild-type enzyme | Escherichia coli |
| 1.01 | - |
purified recombinant mutant F228E | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protein + H2O | - |
Escherichia coli | peptides | - |
? | |
| protein sigma32 + H2O | regulatory protein | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | - |
Escherichia coli |
| More | highly conserved residues Phe228 and Gly230 lie in the central pore region of the hexamer | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FtsH | - |
Escherichia coli |
| M41.001 | Merops-ID | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 42 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Escherichia coli | |
| ATPgammaS | wild-type enzyme and mutants, dependent on protein substrate, low activity | Escherichia coli | |
| additional information | no activity with ADP, wild-type enzyme and mutants | Escherichia coli |
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