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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Chemistry & biology

Functional plasticity and allosteric regulation of α-ketoglutarate decarboxylase in central mycobacterial metabolism

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Chemistry & biology - 26 Aug 2011

Wagner T, Bellinzoni M, Wehenkel A, O'Hare HM, Alzari PM

Link to Pubmed [PMID] – 21867916

Chem. Biol. 2011 Aug;18(8):1011-20

The α-ketoglutarate dehydrogenase (KDH) complex is a major regulatory point of aerobic energy metabolism. Mycobacterium tuberculosis was reported to lack KDH activity, and the putative KDH E1o component, α-ketoglutarate decarboxylase (KGD), was instead assigned as a decarboxylase or carboligase. Here, we show that this protein does in fact sustain KDH activity, as well as the additional two reactions, and these multifunctional properties are shared by the Escherichia coli homolog, SucA. We also show that the mycobacterial enzyme is finely regulated by an additional acyltransferase-like domain and by the action of acetyl-CoA, a powerful allosteric activator able to enhance the concerted protein motions observed during catalysis. Our results uncover the functional plasticity of a crucial node in bacterial metabolism, which may be important for M. tuberculosis during host infection.

http://www.ncbi.nlm.nih.gov/pubmed/21867916