A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units

10.1038/862 ◽  
1998 ◽  
Vol 5 (7) ◽  
pp. 602-611 ◽  
Author(s):  
Bin Ren ◽  
Gudrun Tibbelin ◽  
Donatella de Pascale ◽  
Mosè Rossi ◽  
Simonetta Bartolucci ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide

scholarly journals A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units

10.1038/2766 ◽  
1998 ◽  
Vol 5 (10) ◽  
pp. 924-924 ◽  
Author(s):  
Bin Ren ◽  
Gudrun Tibbelin ◽  
Donatella de Pascale ◽  
Mosè Rossi ◽  
Simonetta Bartolucci ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide

scholarly journals Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus

2004 ◽  
Vol 271 (16) ◽  
pp. 3437-3448 ◽  
Author(s):  
Emilia Pedone ◽  
Bin Ren ◽  
Rudolf Ladenstein ◽  
Mosè Rossi ◽  
Simonetta Bartolucci
Keyword(s):  
Functional Properties ◽  
Pyrococcus Furiosus ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide

scholarly journals Activation of choleragen by thiol: protein disulfide oxidoreductase.

1980 ◽  
Vol 255 (23) ◽  
pp. 11085-11087
Author(s):  
J. Moss ◽  
S.J. Stanley ◽  
J.E. Morin ◽  
J.E. Dixon
Keyword(s):  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide ◽  
Thiol Protein

Insights on a New PDI-like Family: Structural and Functional Analysis of a Protein Disulfide Oxidoreductase from the Bacterium Aquifex aeolicus

2006 ◽  
Vol 356 (1) ◽  
pp. 155-164 ◽  
Author(s):  
Emilia Pedone ◽  
Katia D'Ambrosio ◽  
Giuseppina De Simone ◽  
Mosè Rossi ◽  
Carlo Pedone ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Aquifex Aeolicus ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide

Thiol–Protein Disulfide Oxidoreductase Activity in Human Placental Tissue Homogenates

1972 ◽  
Vol 50 (5) ◽  
pp. 507-509 ◽  
Author(s):  
Luis A. Branda ◽  
Barbara M. Ferrier ◽  
Lynne Celhoffer
Keyword(s):  
Placental Tissue ◽  
Enzymic Activity ◽  
Ph Optimum ◽  
Rapid Reduction ◽  
Oxidoreductase Activity ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Human Placental Tissue ◽  
Protein Disulfide ◽  
Thiol Protein

Thiol–protein disulfide oxidoreductase activity was detected in the soluble cell fraction of human placental tissue homogenized in sucrose. This activity was demonstrated in the rapid reduction of oxytocin and the somewhat less rapid reduction of insulin by reduced glutathione. The apparent pH optimum of the enzymic activity for the reduction of oxytocin and insulin was found to be near pH 8.

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