Constituents of cinnamon inhibit bacterial acetyl CoA carboxylase

Glen Meades, Rachel L. Henken, Grover L. Waldrop, Md Mukhlesur Rahman, S. Douglass Gilman, Guy P. P. Kamatou, Alvaro M. Viljoen, Simon Gibbons

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21 Citations (Scopus)


Cinnamon bark (Cinnamomum zeylanicum) is used extensively as an antimicrobial material and currently is being increasingly used in Europe by people with type II diabetes to control their glucose levels. In this paper we describe the action of cinnamon oil, its major component, trans-cinnamaldehyde, and an analogue, 4-hydroxy-3-methoxy-trans-cinnamaldehyde against bacterial acetyl-CoA carboxylase in an attempt to elucidate the mechanism of action of this well-known antimicrobial material. These natural products inhibited the carboxyltransferase component of Escherichia coli acetyl-CoA carboxylase but had no effect on the activity of the biotin carboxylase component. The inhibition patterns indicated that these products bound to the biotin binding site of carboxyltransferase with trans-cinnamaldehyde having a Kvalue of 3.80.6mM. The inhibition of carboxyltransferase by 4-hydroxy-3-methoxy-trans-cinnamaldehyde was analyzed with a new assay for this enzyme based on capillary electrophoresis. These results explain, in part, the antibacterial activity of this well-known antimicrobial material.

Original languageEnglish
Pages (from-to)1570-1575
Number of pages6
JournalPlanta Medica
Issue number14
Early online date8 Apr 2010
Publication statusPublished - 11 Oct 2010


  • acetylCoA carboxylase
  • carboxyltransferase
  • Cinnamomum zeylanicum
  • Lauraceae
  • trans cinnamaldehyde

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