a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase

C.W. Levy, C. Baldock, A.J. Wallace, S. Sedelnikova, R.C. Viner, J.M. Clough, A.R. Stuitje, A.R. Slabas, D.W. Rice, J.B. Rafferty

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    Enoyl acyl carrier protein (ACP) reductase catalyses the last reductive step of fatty acid biosynthesis, reducing the enoyl group of a growing fatty acid chain attached to ACP to its acyl product using NAD(P)H as the cofactor. This enzyme is the target for the diazaborine class of anti-bacterial agents, the biocide triclosan, and one of the targets for the front-line anti-tuberculosis drug isoniazid. The structures of complexes of Escherichia coli enoyl-ACP reductase (ENR) from crystals grown in the presence of NAD
    Original languageEnglish
    Pages (from-to)171-180
    JournalJournal of Molecular Biology
    Volume309
    Issue number1
    DOIs
    Publication statusPublished - 2001

    Fingerprint

    Dive into the research topics of 'a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase'. Together they form a unique fingerprint.

    Cite this