Constituents of cinnamon inhibit bacterial acetyl CoA carboxylase

Meades, Glen, Henken, Rachel L., Waldrop, Grover L., Rahman, Md Mukhlesur, Gilman, S. Douglass, Kamatou, Guy P. P., Viljoen, Alvaro M. and Gibbons, Simon (2010) Constituents of cinnamon inhibit bacterial acetyl CoA carboxylase. Planta Medica, 76 (14). pp. 1570-1575. ISSN 0032-0943

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: acetylcoa carboxylase,carboxyltransferase,cinnamomum zeylanicum,lauraceae,trans cinnamaldehyde,analytical chemistry,molecular medicine,pharmacology,pharmaceutical science,drug discovery,complementary and alternative medicine,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1600/1602
Faculty \ School: Faculty of Science > School of Pharmacy
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Depositing User: LivePure Connector
Date Deposited: 15 Jul 2020 23:39
Last Modified: 15 Jul 2020 23:39
URI: https://ueaeprints.uea.ac.uk/id/eprint/76130
DOI: 10.1055/s-0030-1249778

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