Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | cPrx I and cPrx II function both as peroxidases and as molecular chaperones. The peroxidase function predominates in the lower molecular weight forms, whereas the chaperone function predominates in the higher molecular weight complexes. Oxidative stress and heat shock exposure of yeasts cause the protein structures of cPrxl and cPrx II to shift from low MW species to high molecular weight complexes. This triggers a peroxidase-to-chaperone functional switch | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | recombinant cPrx I produces in Escherichia coli forms differently sized high molecular weight protein structures. cPrx I and cPrx II function both as peroxidases and as molecular chaperones. The peroxidase function predominates in the lower molecular weight forms, whereas the chaperone function predominates in the higher molecular weight complexes. Oxidative stress and heat shock exposure of yeasts cause the protein structures of cPrxl and cPrx II to shift from low MW species to high molecular weight complexes. This triggers a peroxidase-to-chaperone functional switch | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
cPrx I | - |
Saccharomyces cerevisiae |
cPrx II | - |
Saccharomyces cerevisiae |
Prx | - |
Saccharomyces cerevisiae |