Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2

Ram Prasad Bhusal, Wanting Jiao, Brooke X. C. Kwai, Jóhannes Reynisson, Annabelle J. Collins, Jonathan Sperry (), Ghader Bashiri () and Ivanhoe K. H. Leung ()
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Ram Prasad Bhusal: The University of Auckland
Wanting Jiao: Victoria University of Wellington
Brooke X. C. Kwai: The University of Auckland
Jóhannes Reynisson: The University of Auckland
Annabelle J. Collins: The University of Auckland
Jonathan Sperry: The University of Auckland
Ghader Bashiri: The University of Auckland
Ivanhoe K. H. Leung: The University of Auckland

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: Abstract Isocitrate lyase is important for lipid utilisation by Mycobacterium tuberculosis but its ICL2 isoform is poorly understood. Here we report that binding of the lipid metabolites acetyl-CoA or propionyl-CoA to ICL2 induces a striking structural rearrangement, substantially increasing isocitrate lyase and methylisocitrate lyase activities. Thus, ICL2 plays a pivotal role regulating carbon flux between the tricarboxylic acid (TCA) cycle, glyoxylate shunt and methylcitrate cycle at high lipid concentrations, a mechanism essential for bacterial growth and virulence.

Date: 2019
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DOI: 10.1038/s41467-019-12614-7

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