Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm

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

Volumn 106, Issue 5, 2009, Pages 1572-1577

  Eser, Markus ^a   Masip, Lluis ^b,d   Kadokura, Hiroshi ^a,e   Georgiou, George ^c   Beckwith, Jonathan ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

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

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^d GENENTECH INC   (United States)

^e NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Monothiol; Protein oxidation; SRP

Indexed keywords

DSBA PROTEIN; GLUTAREDOXIN; GLUTATHIONE REDUCTASE; OXIDOREDUCTASE; THIOREDOXIN 1; THIOREDOXIN REDUCTASE; DISULFIDE; GLUTATHIONE;

ARTICLE; BACTERIAL STRAIN; BIOSYNTHESIS; CYTOPLASM; DISULFIDE BOND; ESCHERICHIA COLI; HOMEOSTASIS; INTRACELLULAR SPACE; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; WESTERN BLOTTING; BIOCATALYSIS; METABOLISM;

ESCHERICHIA COLI;

BIOCATALYSIS; CYTOPLASM; DISULFIDES; ESCHERICHIA COLI; GLUTAREDOXINS; GLUTATHIONE; OXIDATION-REDUCTION; PERIPLASM;

EID: 60849121135     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0812596106     Document Type: Article

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