1. Adelaide Research & Scholarship
  2. Schools and Disciplines
  3. School of Chemistry and Physics
  4. Chemistry and Physics publications
Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/139080
Citations
Scopus Web of Science® Altmetric
?
?
Full metadata record
DC FieldValueLanguage
dc.contributor.authorDoherty, D.Z.-
dc.contributor.authorGhith, A.-
dc.contributor.authorHo, A.-
dc.contributor.authorDe Voss, J.J.-
dc.contributor.authorBell, S.G.-
dc.date.issued2023-
dc.identifier.citationChemical Communications, 2023; 59(61):9392-9395-
dc.identifier.issn1359-7345-
dc.identifier.issn1364-548X-
dc.identifier.urihttps://hdl.handle.net/2440/139080-
dc.description.abstractCholesterol catabolism is an important survival mechanism for the pathogenic Mycobacterium tuberculosis. Various other mycobacteria degrade not only cholesterol but plant sterols such as sitosterol and campesterol. In this work we demonstrate that the cytochrome P450 (CYP) CYP125 enzyme family is capable of sitosterol and campesterol side-chain oxidation and activation in these bacteria. We also show that the CYP142 and CYP124 cholesterol hydroxylating enzyme families are significantly less active for sitosterol hydroxylation compared to CYP125 enzymes.-
dc.description.statementofresponsibilityDaniel Z. Doherty, Amna Ghith, Ava Ho, James J. De Voss and Stephen G. Bell-
dc.language.isoen-
dc.publisherRoyal Society of Chemistry-
dc.rights© The Royal Society of Chemistry 2023.-
dc.source.urihttp://dx.doi.org/10.1039/d3cc02312e-
dc.subjectMycobacterium tuberculosis-
dc.subjectCholesterol-
dc.subjectSitosterols-
dc.subjectCytochrome P-450 Enzyme System-
dc.subjectOxidation-Reduction-
dc.subject.meshMycobacterium tuberculosis-
dc.subject.meshCholesterol-
dc.subject.meshSitosterols-
dc.subject.meshCytochrome P-450 Enzyme System-
dc.subject.meshOxidation-Reduction-
dc.titleThe bacterial cytochrome P450 (CYP) CYP125 enzymes can competitively oxidise sitosterol in the presence of cholesterol-
dc.typeJournal article-
dc.identifier.doi10.1039/d3cc02312e-
dc.relation.granthttp://purl.org/au-research/grants/arc/DP210103970-
pubs.publication-statusPublished-
dc.identifier.orcidGhith, A. [0000-0003-1753-6939]-
dc.identifier.orcidBell, S.G. [0000-0002-7457-9727]-
Appears in Collections:Chemistry and Physics publications

Files in This Item:
There are no files associated with this item.
Show simple item record


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.