Bacitracin inhibits the reductive activity of protein disulfide isomerase by disulfide bond formation with free cysteines in the substrate-binding domain

FEBS Journal

Volumn 278, Issue 12, 2011, Pages 2034-2043

  Dickerhof, Nina ^a   Kleffmann, Torsten ^a   Jack, Ralph ^a   McCormick, Sally ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

bacitracin; cyclic peptide; protein disulfide isomerase; protein disulfide isomerase (PDI) inhibition; substrate binding domain; thiol disulfide exchange

Indexed keywords

BACITRACIN; BACITRACIN A; BACITRACIN F; BACITRACIN H; CYSTEINE; INSULIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN DISULFIDE ISOMERASE; THIOL; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DISULFIDE BOND; DRUG MECHANISM; DRUG PURIFICATION; ENZYME INHIBITION; ENZYME SUBSTRATE COMPLEX; IC 50; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN DOMAIN;

ANIMALS; BACITRACIN; CATALYTIC DOMAIN; CATTLE; CYSTEINE; DISULFIDES; ENZYME INHIBITORS; MOLECULAR STRUCTURE; PROTEIN DISULFIDE-ISOMERASES; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 79958122391     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08119.x     Document Type: Article

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