NDLI: Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding.

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Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schmid, F. X. Schönbrunner, E. R.
Description	Author Affiliation: Schönbrunner ER ( Biochemisches Laboratorium, Universität Bayreuth, Federal Republic of Germany.);
Abstract	The cis-trans isomerization of prolyl peptide bonds and the formation of disulfide bonds are both slow steps in protein folding. By using ribonuclease T1 as a model system, we show that these two processes can become linked in the oxidative folding of reduced proteins and that the formation of the correct disulfide bonds is facilitated in the presence of peptidyl-prolyl cis-trans isomerase. In particular, the efficiency of protein disulfide isomerase (EC 5.3.4.1) as a catalyst of disulfide bond formation in the course of oxidative folding is markedly improved when peptidyl-prolyl cis-trans isomerase is present simultaneously. Possibly, unfolded or partially folded protein chains with correct prolyl isomers are better substrates for catalysis by protein disulfide isomerase. The interdependence of the two enzymatic activities detected during in vitro folding experiments could be of importance for the de novo folding and disulfide bond formation of nascent proteins in the endoplasmic reticulum.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acid Isomerases Metabolism Carrier Proteins Isomerases Protein Conformation Ribonuclease T1 Animals Cloning, Molecular Escherichia Coli Enzymology Genetics Kinetics Liver Oxidation-Reduction Peptidylprolyl Isomerase Protein Denaturation Protein Disulfide-Isomerases Recombinant Proteins Chemistry Time Factors Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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