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disulfide oxidoreductase activity

Known as: disulphide oxidoreductase activity 
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds. [MetaCyc:DISULFOXRED-RXN]
National Institutes of Health

Papers overview

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2014
2014
Background: Thioredoxins ("TRX") are ubiquitous 12-kDa oxidoreductase enzyme containing a dithiol-disulfide active site… 
Highly Cited
2005
Highly Cited
2005
DsbA proteins, the primary catalysts of protein disulfide bond formation, are known to affect virulence and penicillin resistance… 
Highly Cited
2003
Highly Cited
2003
ABSTRACT Disulfide oxidoreductases are viewed as foldases that help to maintain proteins on productive folding pathways by… 
Highly Cited
1998
Highly Cited
1998
The application of an automated method for the screening of protein activity based on the sequence-to-structure-to-function… 
Highly Cited
1992
Highly Cited
1992
Glutaredoxin is essential for the glutathione (GSH)-dependent synthesis of deoxyribonucleotides by ribonucleotide reductase, and… 
Highly Cited
1988
Highly Cited
1988
Highly Cited
1983
Highly Cited
1983
The protein disulphide-bond isomerization activity of highly active homogeneous protein disulphide-isomerase (measured by re… 
Highly Cited
1979
Highly Cited
1979
  • A. Holmgren
  • Journal of Biological Chemistry
  • 1979
  • Corpus ID: 11371465
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative…