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

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Show simple item record Bhusal, Ram Prasad en Jiao, Wanting en Kwai, Brooke en Reynisson, Johannes en Collins, Annabelle J en Sperry, Jonathan en Bashiri, Ghader en Leung, Ka Ho Ivanhoe en 2019-11-26T02:31:28Z en 2019-10-11 en
dc.identifier.citation Nature communications 10(1):4639 11 Oct 2019 en
dc.identifier.issn 2041-1723 en
dc.identifier.uri en
dc.description.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. en
dc.format.medium Electronic en
dc.language eng en
dc.relation.ispartofseries Nature communications en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. en
dc.rights.uri en
dc.rights.uri en
dc.title Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2. en
dc.type Journal Article en
dc.identifier.doi 10.1038/s41467-019-12614-7 en
pubs.issue 1 en
pubs.begin-page 4639 en
pubs.volume 10 en
dc.rights.holder Copyright: The authors en
pubs.publication-status Published en
dc.rights.accessrights en
pubs.subtype Research Support, Non-U.S. Gov't en
pubs.subtype research-article en
pubs.subtype Journal Article en
pubs.elements-id 784192 en Science en Biological Sciences en Chemistry en Science Research en Maurice Wilkins Centre (2010-2014) en
dc.identifier.eissn 2041-1723 en
pubs.record-created-at-source-date 2019-10-13 en
pubs.dimensions-id 31604954 en

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