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Candidemia incidence has been rising worldwide following increases in fungicide-resistant pathogens highlighting the need for more effective antifungal agents with novel modes of action. The membrane-bound enzyme alternative oxidase (AOX) promotes fungicide resistance and is absent in humans making it a desirable therapeutic target. However, the lipophilic nature of the AOX substrate (ubiquinol-10) has hindered its kinetic characterisation in physiologically-relevant conditions. Here, we present the purification and expression of recombinant AOXs from <jats:italic>C. albicans<\/jats:italic> and <jats:italic>C. auris<\/jats:italic> in a self-assembled proteoliposome (PL) system. Kinetic parameters (K<jats:sub>m<\/jats:sub> and V<jats:sub>max<\/jats:sub>) with respect to ubiquinol-10 have been determined. The PL system has also been employed in dose\u2013response assays with novel AOX inhibitors. Such information is critical for the future development of novel treatments for Candidemia.<\/jats:p>","DOI":"10.1038\/s41598-021-94320-3","type":"journal-article","created":{"date-parts":[[2021,7,20]],"date-time":"2021-07-20T10:26:57Z","timestamp":1626776817000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Kinetic characterisation and inhibitor sensitivity of Candida albicans and Candida auris recombinant AOX expressed in a self-assembled proteoliposome system"],"prefix":"10.1038","volume":"11","author":[{"given":"Alice C.","family":"Copsey","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mario R. 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