Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase.
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.
Institutionen för Fysik och Mätteknik/Department of Chemistry, Linköping University, Sweden.
P O
PO
Freskgård
N
N
Bergenhem
B H
BH
Jonsson
M
M
Svensson
U
U
Carlsson
D000591:Amino Acid Isomerases / Q000378:metabolism*; D002256:Carbonic Anhydrases / Q000648:ultrastructure*; D002352:Carrier Proteins / Q000378:metabolism*; D018833:Chaperonins; D006801:Humans; D007535:Isomerases / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase; D011392:Proline / Q000737:chemistry; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism*; D013997:Time Factors
D002352:Carrier Proteins; D011506:Proteins; D011392:Proline; D018833:Chaperonins; D002256:Carbonic Anhydrases; D007535:Isomerases; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase