Folding catalyst

Gothel, S.F. and Marahiel, M.A. (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cellular and Molecular Life Sciences 55, 423-436. 

The p(25-35) interacts with the native protein, destroys its native conformation, and forms pathological aggregates. Its action is exactly opposite to that of a chaperone, which helps proteins fold correctly. Hence, p(25-35) is termed as an antichaperone, protein disulphide isomerase (PDI), a folding catalyst and chaperone, under certain conditions, can facilitate the... 

In Molecular Chaperones and Folding Catalysts. Regulation, Cellular Function and Mechanism (B. Bukau, ed.), pp. 573-607. Harwood Academic Publishers, Amsterdam. 

Thress, K., Song, J., Morimoto, R. I., and Kornbluth, S. (2001). EMBO J. 20, 1033-1041. Toft, D. O. (1999). In Molecular Chaperones and Folding Catalysts. Regulation, Cellular Function and Mechanism (B. Bukau, ed.), pp. 313-327. Harwood Academic Publishers, Amsterdam. 

Gething, M.-J. (1997). Guidebook to Molecular Chaperones and Protein Folding Catalysts. Oxford University Press, New York. 

Other important protein-folding catalysts In the ER lumen are peptldyl-prolyl isomerases, a family of enzymes that accelerate the rotation about peptidyl-prolyl bonds in unfolded segments of a polypeptide ... 

Improperly Folded Proteins in the ER Induce Expression of Protein-Folding Catalysts... 

The accumulation of abnormally folded proteins and unassembled subunits in the ER can induce increased expression of ER protein-folding catalysts via the unfolded-proteln response (see Figure 16-22). 

Lindquist, S., and Schirmer, E.C. 1999. The Role of Hspl04 in Stress Tolerance and Prion Maintenance. In Molecular Chaperones and Folding Catalysts. Regulation,... 

Fig. 15.2 Mechanism of CO oxidation on supported fold catalysts, as proposed by Plaruta et al. [16].

The disulfide formation depends on the protein conformation that places Cys residues into appropriate proximity and the disulfide redox potential that determines the intrinsic stability of protein disulfide bonds. For catalytic activity, the reduced dithiol form of protein disulfide isomerase is required. Protein disulfide isomerase is a folding catalyst that assists protein folding (Gilbert, 1997). The enzyme increases the rate of the overall folding process of the substrate protein without altering its pathway. 

Relationship with other ER Chaperones and Folding Catalysts 1007... 

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