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Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase
- Source :
- Science. 258:466-468
- Publication Year :
- 1992
- Publisher :
- American Association for the Advancement of Science (AAAS), 1992.
-
Abstract
- Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a chaperone. This function is exerted on an early folding intermediate of carbonic anhydrase, which is thereby prevented from aggregating, whereas the isomerase activity is performed later in the folding process.
- Subjects :
- Protein Denaturation
Time Factors
Isomerase activity
Chaperonins
Proline
Cell
Isomerase
Carbonic anhydrase
Prolyl isomerase
medicine
Humans
Chaperone activity
Isomerases
Amino Acid Isomerases
Carbonic Anhydrases
chemistry.chemical_classification
Multidisciplinary
biology
Proteins
Peptidylprolyl Isomerase
Protein Structure, Tertiary
Enzyme
medicine.anatomical_structure
chemistry
Biochemistry
Chaperone (protein)
biology.protein
Carrier Proteins
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 258
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....3192a4b8aa0d04a88a9dd45d48a42cfc
- Full Text :
- https://doi.org/10.1126/science.1357751