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Warfarin analogs target disulfide bond-forming enzymes and suggest a residue important for quinone and coumarin binding

2024-02-19

Abstract excerpt

Disulfide bond formation has a central role in protein folding of both eukaryotes and prokaryotes. DsbB and VKOR enzymes catalyze the oxidation of the oxidoreductase partner and the formation of de novo disulfide bonds using quinone as cofactor. We have used E. coli and a family of warfarin analogs to study de novo disulfide bond formation. We found that human VKORc1 can function in E. coli by removing two positiv...

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Identifiers and source

Literature Corpus work
9f0c1803-3ca6-5a60-ac40-87a4ce77ac48
DOI
10.1101/2024.02.18.580799
Open publication

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Warfarin analogs target disulfide bond-forming enzymes and suggest a residue important for quinone and coumarin bindingDOI 10.1101/2024.02.18.580799
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