Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 27, 2004, Pages 10018-10023

  Segatori, Laura ^a   Paukstelis, Paul J ^b   Gimbert, Hiram F ^a   Georgiou, George ^a,b,c  

^a The University of Texas at Austin   (United States)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYSTEINE; DSBA PROTEIN; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN DSBC; PROTEIN DSBD; THIOREDOXIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CATALYSIS; CATALYST; CHIMERA; CYTOPLASM; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; ISOMERIZATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN DOMAIN; REDUCTION;

CATALYSIS; DIMERIZATION; DISULFIDES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN ENGINEERING; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 3042709650     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0403003101     Document Type: Article

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