Enzymes that catalyse the restructuring of proteins.
The large enzyme families of protein disulfide isomerases and peptidyl prolyl cis/trans isomerases have been shown to assist polypeptide restructuring. Various folding states of polypeptides may serve as substrates of the catalysed reaction. Our understanding of the cellular function of these enzymes is increasing as a result of the availability of more specific inhibitors, the discovery of natural substrates and the use of genetically modified organisms. Further highlights of these studies include insights into the three-dimensional structures of enzyme-ligand complexes, as well as into the mechanism of slow folding phases on the atomic level.
Schiene
C
C
Research Unit Enzymology of Protein Folding, Max-Planck Society, Halle/Saale, D-06120, Germany.
Fischer
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G
D000818:Animals; D002384:Catalysis; D016572:Cyclosporine / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004798:Enzymes / Q000502:physiology*; D006801:Humans; D020104:Immunophilins / Q000502:physiology; D051379:Mice; D008954:Models, Biological; D018832:Molecular Chaperones / Q000502:physiology; D011487:Protein Conformation / Q000187:drug effects; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology; D022021:Tacrolimus Binding Proteins
D004791:Enzyme Inhibitors; D004798:Enzymes; D018832:Molecular Chaperones; D016572:Cyclosporine; D022021:Tacrolimus Binding Proteins; D020104:Immunophilins