A Kinetic Analysis of the Folding of Human Carbonic Anhydrase II and Its Catalysis by Cyclophilin (*)
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Summary
The kinetics of unfolding and refolding of human carbonic anhydrase II and its catalysis by the peptidyl-prolyl-cis/trans-isomerase cyclophilin were investigated and it was found that some prolyl peptide bonds isomerize early in refolding, at the stage of the molten globule and as a consequence, molecules with incorrect prolyL isomers are formed in competition with the productive folding of Uf.
- Type
- article
- Published
- 1995-01-13
- Cited by
- 67
- References
- 31
- Access
- Open access
- OpenAlex
- https://openalex.org/W2001101609
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:20106006
Keywords
Chemistry, Prolyl isomerase, Isomerization, Molten globule, Peptidylprolyl isomerase
References
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- Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum.
- Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase.
- The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen.
- Catalysis of proline isomerization during protein-folding reactions.
- Conformational transitions of thioredoxin in guanidine hydrochloride.
- Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis.
- Characterization of folding intermediates using prolyl isomerase.
- Catalysis of protein folding by prolyl isomerase
- Enzymatic catalysis of prolyl isomerization in an unfolding protein.
- Reactivation of kinetics of guanidine denatured bovine carbonic anhydrase B.
- Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase.
- Calculation of protein extinction coefficients from amino acid sequence data.
- Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization.
- Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.
- The cyclophilin homolog ninaA is required in the secretory pathway.
- Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions.
- Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding
Cited by
- X-Ray Structures and Analysis of 11 Cyclosporin Derivatives Complexed with Cyclophilin A.
- Folding and stability of human carbonic anhydrase II.
- A ribosome‐associated peptidyl‐prolyl cis/trans isomerase identified as the trigger factor.
- As Chlamydomonas reinhardtii acclimates to low-CO2 conditions there is an increase in cyclophilin expression
- T cell signaling: biochemical and structural characterization of Itk, CypA and HS1.
- Effects of ligand binding on the rigidity and mobility of proteins : a computational and experimental approach
- Subtractive hybridization analysis of gastric diseases-associated Helicobacter pylori identifies peptidyl-prolyl isomerase as a potential marker for gastric cancer.
- Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins
- Cyclosporin A inhibits inositol 1,4,5-trisphosphate binding to its receptors and release of calcium from intracellular stores in peritoneal macrophages.
- Cyclophilin-promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme.
- Identification of all FK506-binding proteins from Neurospora crassa.
- The rate‐limiting steps for the folding of an antibody scFv fragment
- A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules.
- Immunophilins: for the love of proteins
- Parallel pathways in the folding of a short-term denatured scFv fragment of an antibody.
- Assisted folding of D‐glyceraldehyde‐3‐phosphate dehydrogenase by trigger factor
- Cloning, characterization and functional expression of a cyclophilin of Entamoeba histolytica.
- Identification and Comparative Analysis of the Peptidyl-Prolyl cis/trans Isomerase Repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe
- Isolation, characterization and targeted disruption of mouse ppia: cyclophilin A is not essential for mammalian cell viability.
- Evidence for isomerization in myotoxin a from the prairie rattlesnake (Crotalus viridis viridis).
Related papers
- Prolyl isomerases.
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- Crosstalk of prolyl isomerases, Pin1/Ess1, and cyclophilin A.
- Structural and Biochemical Characterization of the Human Cyclophilin Family of Peptidyl-Prolyl Isomerases
- An endoplasmic reticulum-specific cyclophilin
- Small Molecule Inhibitors of Peptidylprolyl cis/trans Isomerase