Adelaide Research & Scholarship
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https://hdl.handle.net/2440/139080
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| Type: | Journal article |
| Title: | The bacterial cytochrome P450 (CYP) CYP125 enzymes can competitively oxidise sitosterol in the presence of cholesterol |
| Author: | Doherty, D.Z. Ghith, A. Ho, A. De Voss, J.J. Bell, S.G. |
| Citation: | Chemical Communications, 2023; 59(61):9392-9395 |
| Publisher: | Royal Society of Chemistry |
| Issue Date: | 2023 |
| ISSN: | 1359-7345 1364-548X |
| Statement of Responsibility: | Daniel Z. Doherty, Amna Ghith, Ava Ho, James J. De Voss and Stephen G. Bell |
| Abstract: | Cholesterol 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. |
| Keywords: | Mycobacterium tuberculosis Cholesterol Sitosterols Cytochrome P-450 Enzyme System Oxidation-Reduction |
| Rights: | © The Royal Society of Chemistry 2023. |
| DOI: | 10.1039/d3cc02312e |
| Grant ID: | http://purl.org/au-research/grants/arc/DP210103970 |
| Published version: | http://dx.doi.org/10.1039/d3cc02312e |
| Appears in Collections: | Chemistry and Physics publications |
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