A hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii

2003 ◽  
Vol 418 (2) ◽  
pp. 179-185 ◽  
Author(s):  
Yasuhiro Kashima ◽  
Kazuhiko Ishikawa
Keyword(s):  
Thioredoxin Reductase ◽  
Pyrococcus Horikoshii ◽  
Hyperthermophilic Archaeon ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide ◽  
Novel Protein

scholarly journals Enzymatic Antioxidant Signatures in Hyperthermophilic Archaea

Antioxidants ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 703 ◽  
Author(s):  
Emilia Pedone ◽  
Gabriella Fiorentino ◽  
Simonetta Bartolucci ◽  
Danila Limauro
Keyword(s):  
Superoxide Radical ◽  
Redox Homeostasis ◽  
Thioredoxin Reductase ◽  
Industrial Applications ◽  
Hyperthermophilic Archaea ◽  
Biological Macromolecules ◽  
Oxygen Species ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide

To fight reactive oxygen species (ROS) produced by both the metabolism and strongly oxidative habitats, hyperthermophilic archaea are equipped with an array of antioxidant enzymes whose role is to protect the biological macromolecules from oxidative damage. The most common ROS, such as superoxide radical (O2•−) and hydrogen peroxide (H2O2), are scavenged by superoxide dismutase, peroxiredoxins, and catalase. These enzymes, together with thioredoxin, protein disulfide oxidoreductase, and thioredoxin reductase, which are involved in redox homeostasis, represent the core of the antioxidant system. In this review, we offer a panorama of progression of knowledge on the antioxidative system in aerobic or microaerobic (hyper)thermophilic archaea and possible industrial applications of these enzymes.

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.

scholarly journals Crystal structure of a protein disulfide oxidoreductase fromAquifex aeolicus

2005 ◽  
Vol 61 (a1) ◽  
pp. c206-c206
Author(s):  
K. D'Ambrosia ◽  
G. De Simone ◽  
E. Pedone ◽  
M. Rossi ◽  
S. Bartolucci ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide
Sign in / Sign up

Export Citation Format

Share Document