Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
38000 | - |
dimer, gel filtration | Escherichia coli |
195000 | - |
decamer, gel filtration | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
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 | Comment | Organism |
---|---|---|
AhpC | - |
Escherichia coli |
alkyl hydroperoxide reductase subunit C | - |
Escherichia coli |
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 |