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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

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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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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 …
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    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0089Oxidoreductases (1.) acting on superoxide as acceptor (1.15)
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    • G01MEASURING; TESTING
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