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Literature summary for 3.4.24.B17 extracted from
- Roles of homooligomerization and membrane association in ATPase and proteolytic activities of FtsH in vitro (2001), Biochemistry, 40, 7687-7693.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dimethylsulfoxid | induces conformational changes, stimulates with SecY s substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate | Escherichia coli |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-Myc-tagged wild-type and mutant enzymes from strain TY024 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of mutants by deletion of N-terminal membrane region, replacement by a leucine-zipper, or replacement by a lactose permease transmembrane segment, the matated proteins show very low remaining activity, but are stimulated by dimethylsulfoxide, the deletion mutant does not show ATPase and proteolytic activity | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ATP | inhibitory at high concentration in presence of dimethylsulfoxide | Escherichia coli | |
| Dimethylsulfoxide | induces conformational changes, stimulates with SecY as substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate | Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasmic membrane | the N-terminus mediates membrane association as well as homooligomeric interaction | Escherichia coli | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | metalloprotease | Escherichia coli |
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 His-Myc-tagged wild-type and mutant enzymes | Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| proteolytic degradation of proteins | degradation of soluble and integral membrane proteins | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | resorufin-labeled substrate | Escherichia coli | ? | - |
? | |
| PhoA protein + H2O | - |
Escherichia coli | ? | - |
? | |
| protein + H2O | - |
Escherichia coli | peptides | - |
? | |
| protein + H2O | substrate binding by the cytoplasmic domain | Escherichia coli | peptides | - |
? | |
| SecY protein + H2O | - |
Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the N-terminus mediates membrane association as well as homooligomeric interaction | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| M41.001 | Merops-ID | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
ATPase activity assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.1 | - |
ATPase activity assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on, induces conformational changes by binding irrespective of ATP hydrolysis | Escherichia coli | |
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