Loading...
Please wait, while we are loading the content...
Similar Documents
A mechanism of drug action revealed by structural studies of enoyl reductase.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Baldock, Clair Baker, Patrick J. Hawkes, Timothy Robert |
| Copyright Year | 1996 |
| 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. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://science.sciencemag.org/content/sci/274/5295/2107.full.pdf |
| PubMed reference number | 8953047v1 |
| Volume Number | 274 |
| Issue Number | 5295 |
| Journal | Science |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Analog Antitubercular Agents Boron Chemistry, Pharmaceutical Covalent Interaction Dinucleoside Phosphates Fatty Acids Fatty acid biosynthetic process Generic Drugs Hydroxyl Radical Niacinamide Nicotinamide adenine dinucleotide (NAD) Oxidoreductase Ribose Sulfur-Sulfur Bond Isomerases genetic linkage isoniazid nicotinamide-beta-riboside |
| Content Type | Text |
| Resource Type | Article |
