The mechanism of action of bacimethrin, a naturally occurring thiamin antimetabolite
| Autor: | Jonathan S. Melnick, Jian-ming Lee, Jason J. Reddick, Soumitra Saha, Tadhg P. Begley, John B. Perkins |
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| Rok vydání: | 2001 |
| Předmět: |
Antimetabolites
Clinical Biochemistry Pharmaceutical Science Dehydrogenase Transketolase Biochemistry Pyrophosphate Gene Expression Regulation Enzymologic Substrate Specificity chemistry.chemical_compound Biosynthesis Drug Discovery Escherichia coli Ketoglutarate Dehydrogenase Complex Thiamine Molecular Biology Antibacterial agent chemistry.chemical_classification Organic Chemistry Oxo-Acid-Lyases food and beverages Enzymes Phosphotransferases (Alcohol Group Acceptor) Pyrimidines Enzyme chemistry Multigene Family Molecular Medicine Thiamine Pyrophosphate human activities Thiamine pyrophosphate |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 11:2245-2248 |
| ISSN: | 0960-894X |
| DOI: | 10.1016/s0960-894x(01)00373-0 |
| Popis: | The mechanism of bacimethrin (2) toxicity has been determined. This compound is converted to 2'-methoxy-thiamin pyrophosphate (10) by the thiamin biosynthetic enzymes. Of the seven thiamin pyrophosphate utilizing enzymes in Escherichia coli, 2'-methoxy-thiamin pyrophosphate inhibits alpha-ketoglutarate dehydrogenase, transketolase, and deoxy-D-xylulose-5-phosphate synthase. Bacimethrin does not cause repression of the genes coding for the thiamin biosynthetic enzymes. |
| Databáze: | OpenAIRE |
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