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Baldock C, et al.  (1996) A mechanism of drug action revealed by structural studies of enoyl reductase. Science 274(5295):2107-10

Abstract: Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.

Status: Published

Type: Journal Article

PubMed ID: 8953047

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Baldock C Rafferty JB Sedelnikova SE Baker PJ Stuitje AR Slabas AR Hawkes TR Rice DW Papers in SGD Colleagues in SGD PubMed Google Scholar

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