Functional properties of PDIA from Aspergillus niger in renaturation of proteins.
Functional properties of protein disulfide isomerase A (PDIA) from Aspergillus niger were investigated using ribonuclease A, glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and prochymosin as substrates. PDIA was shown to function as an isomerase catalyzing the refolding of denatured and reduced ribonuclease A. PDIA also exhibited trx-independent chaperone activity preventing the aggregation of reduced, denatured GAPDH, an enzyme lacking disulfide bonds. Both isomerase activity and chaperone function of PDIA were essential for the efficient refolding of the reduced, denatured prochymosin.
Liang
Yurong
Y
Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China.
Li
Wei
W
Ma
Qing
Q
Zhang
Yuying
Y
D001234:Aspergillus niger / Q000201:enzymology* / Q000502:physiology*; D012085:Chymosin / Q000737:chemistry / Q000378:metabolism; D004792:Enzyme Precursors / Q000737:chemistry / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000378:metabolism; D018832:Molecular Chaperones / Q000502:physiology; D019704:Protein Disulfide-Isomerases / Q000502:physiology*; D017510:Protein Folding; D020673:Protein Renaturation; D012259:Ribonuclease, Pancreatic / Q000737:chemistry / Q000378:metabolism
D004792:Enzyme Precursors; D018832:Molecular Chaperones; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D012259:Ribonuclease, Pancreatic; C032443:prorennin; D012085:Chymosin; D019704:Protein Disulfide-Isomerases