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Literature summary for 1.11.1.28 extracted from
- Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions (2018), Sci. Rep., 8, 14151 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38000 | - |
dimer, gel filtration | Escherichia coli |
| 195000 | - |
decamer, gel filtration | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| decamer | the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer | Escherichia coli |
| dimer | the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer | Escherichia coli |
| oligomer | heat induces oligomerization of AhpC. At 53°C the oxidized AhpC forms an high-molecular-weight oligomer with a molecular mass of about 2.0-3.0 MDa, corresponding to 100-150 subunits | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AhpC | - |
Escherichia coli |
| alkyl hydroperoxide reductase subunit C | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | alkyl hydroperoxide reductase subunit C acquires chaperone activity under heat stress. High-molecular-weight oligomer formation and the chaperone-like activity of oxidized AhpC depend on the incubation temperature and the period of incubation | Escherichia coli |
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Release 2023.1 (January 2023)
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