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.
Freskgård
P O
PO
Institutionen för Fysik och Mätteknik/Department of Chemistry, Linköping University, Sweden.
Bergenhem
N
N
Jonsson
B H
BH
Svensson
M
M
Carlsson
U
U
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