Inhibitor binding studies on enoyl-reductase reveal conformational changes related to substrate recognition.

A. Roujeinikova, S. Sedelnikova, G.J. de Boer, A.R. Stuitje, A.R. Slabas, J.B. Rafferty, D.W. Rice

    Research output: Contribution to JournalArticleAcademicpeer-review

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    Abstract

    Enoyl acyl carrier protein reductase (ENR) is involved in fatty acid biosynthesis. In Escherichia coli this enzyme is the target for the experimental family of antibacterial agents, the diazaborines, and for triclosan, a broad spectrum antimicrobial agent. Biochemical studies have suggested that the mechanism of diazaborine inhibition is dependent on NAD
    Original languageEnglish
    Pages (from-to)30811-30817
    Number of pages7
    JournalJournal of Biological Chemistry
    Volume274
    DOIs
    Publication statusPublished - 1999

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