Jacobi et al., 1997 - Google Patents
Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA: influence of electrostatic interactions on stability and …Jacobi et al., 1997
View HTML- Document ID
- 16865965749717180678
- Author
- Jacobi A
- Huber-Wunderlich M
- Hennecke J
- Glockshuber R
- Publication year
- Publication venue
- Journal of Biological Chemistry
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Snippet
Disulfide oxidoreductases are structurally related proteins that share the thioredoxin fold and a catalytic disulfide bond that is located at the N terminus of an α-helix. The different redox potentials of these enzymes varying from− 270 mV for thioredoxin to− 125 mV for DsbA have …
- 230000003993 interaction 0 title abstract description 16
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- C07K14/775—Apolipopeptides
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0089—Oxidoreductases (1.) acting on superoxide as acceptor (1.15)
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