The mechanism of action of bacimethrin, a naturally occurring thiamin antimetabolite. Academic Article

abstract

• 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.

authors

• Begley, Tadhg

published proceedings

• Bioorg Med Chem Lett

author list (cited authors)

• Reddick, J. J., Saha, S., Lee, J., Melnick, J. S., Perkins, J., & Begley, T. P.

citation count

• 62

complete list of authors

• Reddick, JJ||Saha, S||Lee, J||Melnick, JS||Perkins, J||Begley, TP

publication date

• September 2001

publisher

• Elsevier  Publisher

published in

• Bioorganic and Medicinal Chemistry Letters  Journal

keywords

• Antimetabolites
• ENZYMES
• Escherichia Coli
• Gene Expression Regulation, Enzymologic
• Ketoglutarate Dehydrogenase Complex
• Multigene Family
• Oxo-acid-lyases
• Phosphotransferases (Alcohol Group Acceptor)
• Pyrimidines
• Substrate Specificity
• Thiamine
• Thiamine Pyrophosphate
• Transketolase

Digital Object Identifier (DOI)

• 10.1016/s0960-894x(01)00373-0

start page

• 2245

end page

• 2248

volume

• 11

issue

• 17

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fs0960-894x%2801%2900373-0