Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/71352
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Type: Journal article
Title: Structure, function and selective inhibition of bacterial acetyl-coa carboxylase
Author: Polyak, S.
Abell, A.
Wilce, M.
Zhang, L.
Booker, G.
Citation: Applied Microbiology and Biotechnology, 2012; 93(3):983-992
Publisher: Springer-Verlag
Issue Date: 2012
ISSN: 0175-7598
1432-0614
Statement of
Responsibility: 
S. W. Polyak, A. D. Abell, M. C. J. Wilce, L. Zhang, G. W. Booker
Abstract: Acetyl-CoA carboxylase (ACC) catalyses the first committed step in fatty acid biosynthesis: a metabolic pathway required for several important biological processes including the synthesis and maintenance of cellular membranes. ACC employs a covalently attached biotin moiety to bind a carboxyl anion and then transfer it to acetyl-CoA, yielding malonyl-CoA. These activities occur at two different subsites: the biotin carboxylase (BC) and carboxyltransferase (CT). Structural biology, together with small molecule inhibitor studies, has provided new insights into the molecular mechanisms that govern ACC catalysis, specifically the BC and CT subunits. Here, we review these recent findings and highlight key differences between the bacterial and eukaryotic isozymes with a view to establish those features that provide an opportunity for selective inhibition. Especially important are examples of highly selective small molecule inhibitors capable of differentiating between ACCs from different phyla. The implications for early stage antibiotic discovery projects, stemming from these studies, are discussed.
Keywords: Acetyl-CoA carboxylase
Enzyme
Inhibition
Antibiotics
Fatty acid biosynthesis
Rights: © Springer-Verlag 2011
DOI: 10.1007/s00253-011-3796-z
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