Enzymes as chaperones and chaperones as enzymes

FEBS Letters

Wang, Chih-Chen¹  Tsou, Chen-Lu¹ 

[1] National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, 15 Datun Road, Beijing 100101, People's Republic of China

关键词: Foldase;    Chaperone;    Protein disulfide isomerase;    Trigger factor;    ATP-dependent protease;    Protein folding;    PDI;    protein disulfide isomerase;    PPI;    peptidyl prolyl cis-trans isomerase;    GAPDH;    d-glyceraldehyde-3-phosphate dehydrogenase;   

DOI  :  10.1016/S0014-5793(98)00272-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown