@article{a9f36f201c0c4c13a6c97a40065f8aba,
title = "Itaconate is a covalent inhibitor of the Mycobacterium tuberculosis isocitrate lyase",
abstract = "Itaconate is a mammalian antimicrobial metabolite that inhibits the isocitrate lyases (ICLs) ofMycobacterium tuberculosis. Herein, we report that ICLs form a covalent adduct with itaconate through their catalytic cysteine residue. These results reveal atomic details of itaconate inhibition and provide insights into the catalytic mechanism of ICLs.",
author = "Kwai, {Brooke X.C.} and Collins, {Annabelle J.} and Middleditch, {Martin J.} and Jonathan Sperry and Ghader Bashiri and Leung, {Ivanhoe K.H.}",
note = "Funding Information: We thank the University of Auckland for funding. A. J. C. was supported by a University of Auckland Doctoral Scholarship. G. B. is supported by a Sir Charles Hercus Fellowship (Health Research Council of New Zealand). We thank Dr Michael Schmitz (The University of Auckland) for maintenance of the NMR spectroscopy facility. This research was undertaken in part using the MX2 beamline at the Australian Synchrotron, part of ANSTO, and made use of the Australian Cancer Research Foundation (ACRF) detector. The coordinates and structure factors have been deposited in the Protein Data Bank under accession code 6XPP. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2020.",
year = "2021",
month = jan,
day = "1",
doi = "10.1039/d0md00301h",
language = "English",
volume = "12",
pages = "57--61",
journal = "RSC Medicinal Chemistry",
issn = "2632-8682",
publisher = "The Royal Society of Chemistry",
number = "1",
}
