scholarly journals Independence of the Chaperone Activity of Protein Disulfide Isomerase from Its Thioredoxin-like Active Site

1995 ◽  
Vol 270 (29) ◽  
pp. 17078-17080 ◽  
Author(s):  
Hui Quan ◽  
Guibao Fan ◽  
Chih-chen Wang
Keyword(s):  
Active Site ◽  
Protein Disulfide Isomerase ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals The Reduction Potential of the Active Site Disulfides of Human Protein Disulfide Isomerase Limits Oxidation of the Enzyme by Ero1α

2010 ◽  
Vol 285 (38) ◽  
pp. 29200-29207 ◽  
Author(s):  
Joseph E. Chambers ◽  
Timothy J. Tavender ◽  
Ojore B. V. Oka ◽  
Stacey Warwood ◽  
David Knight ◽  
...  
Keyword(s):  
Active Site ◽  
Protein Disulfide Isomerase ◽  
Reduction Potential ◽  
Human Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Functional analysis of tunicamycin-inducible gene A polypeptide from Aspergillus niger

2005 ◽  
Vol 83 (5) ◽  
pp. 654-658 ◽  
Author(s):  
Yurong Liang ◽  
Wei Li ◽  
Qing Ma ◽  
Yuying Zhang
Keyword(s):  
Functional Analysis ◽  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Protein Disulfide Isomerase ◽  
Ribonuclease A ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Chaperone Protein ◽  
Protein Disulfide ◽  
Inducible Gene

Tunicamycin-inducible gene A polypeptide (TIGA) is a member of the protein disulfide isomerase (PDI) family and is suggested to facilitate the folding of nascent polypeptides. The functional properties of TIGA were investigated here. TIGA acted as an isomerase, catalyzing the refolding of denatured and reduced ribonuclease A. TIGA also exhibited chaperone activity in the refolding of denatured prochymosin but not in the refolding of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), indicating that it had substrate specificity with respect to chaperone activity. Detailed study with a series of thioredoxin-motif (trx-motif) mutants revealed that the 2 trx-motifs of TIGA were not equal in activity. The N-terminal trx-motif was more active than the C-terminal trx-motif, and the first cysteine in each trx-motif was necessary for isomerase activity.Key words: tunicamycin-inducible gene A polypeptide (TIGA), protein disulfide isomerase, chaperone, protein refolding.

scholarly journals DsbG, a Protein Disulfide Isomerase with Chaperone Activity

2000 ◽  
Vol 275 (18) ◽  
pp. 13349-13352 ◽  
Author(s):  
Feng Shao ◽  
Martin W. Bader ◽  
Ursula Jakob ◽  
James C. A. Bardwell
Keyword(s):  
Protein Disulfide Isomerase ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Ribostamycin Inhibits the Chaperone Activity of Protein Disulfide Isomerase

2001 ◽  
Vol 289 (5) ◽  
pp. 967-972 ◽  
Author(s):  
Tomohisa Horibe ◽  
Hiroaki Nagai ◽  
Keiichi Sakakibara ◽  
Yasunari Hagiwara ◽  
Masakazu Kikuchi
Keyword(s):  
Protein Disulfide Isomerase ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Inhibition of Protein Disulfide Isomerase (PDI) by Nitroarachidonic Acid (NO2-AA): Nitroalkylation of Cys-Active Site Residues

2015 ◽  
Vol 87 ◽  
pp. S44
Author(s):  
Lucia Gonzalez-Perilli ◽  
Mauricio Mastrogiovanni ◽  
Homero Rubbo ◽  
Francisco Laurindo ◽  
Andres Trostchansky
Keyword(s):  
Active Site ◽  
Protein Disulfide Isomerase ◽  
Active Site Residues ◽  
Disulfide Isomerase ◽  
Protein Disulfide
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