Enzymes as chaperones and chaperones as enzymes.
Chaperones and foldases are two groups of accessory proteins which assist maturation of nascent peptides into functional proteins in cells. Protein disulfide isomerase, a foldase, and ATP-dependent proteases, responsible for degradation of misfolded proteins in cells, both have intrinsic chaperone activities. Trigger factor and DnaJ, well known Escherichia coli chaperones, show peptidyl prolyl isomerase and protein disulfide isomerase activities respectively. It is suggested that the combination of chaperone and enzyme activities in one molecule is the result of evolution to increase molecular efficiency.
Wang
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National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, People's Republic of China.
Tsou
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D049069:ATP-Dependent Proteases; D001426:Bacterial Proteins / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase / Q000378:metabolism; D019704:Protein Disulfide-Isomerases / Q000378:metabolism; D017510:Protein Folding; D012697:Serine Endopeptidases / Q000378:metabolism
D001426:Bacterial Proteins; D004798:Enzymes; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D019696:Peptidylprolyl Isomerase; D019704:Protein Disulfide-Isomerases