Abstract
Publisher Summary This chapter discusses the function of prolyl isomerases in protein folding. The importance of prolyl isomerization reactions as slow, rate-limiting steps of folding, and their interdependence with other events in protein folding are described. Some experimental data on the catalysis by prolyl isomerases of various slow in vitro protein folding reactions are reviewed. The enzymatic functions of prolyl isomerases in vitro are fairly well characterized. They catalyze cis-trans isomerizations of Xaa-Pro bonds in small peptides and some proline-limited steps in the slow folding of several proteins. The characterization of the molecular nature of rate-limiting steps is a major aim in the elucidation of the folding mechanism of proteins. Folding reactions that involve prolyl isomerization are identified by measuring their kinetic properties and by comparing them with the properties of prolyl isomerization in short peptides. The chapter also explores the results that possibly suggest a role for prolyl isomerases in cellular folding and a close inter-relationship with disulfide bond formation. The efficiencies of various prolyl isomerases as catalysts of the slow-folding reactions of different proteins under varying folding conditions are tabulated.
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