An Oxygenase-Independent Cholesterol Catabolic Pathway Operates under Oxic Conditions

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Title:	An Oxygenase-Independent Cholesterol Catabolic Pathway Operates under Oxic Conditions
Authors:	王柏翔;Wang, Po-Hsiang;Lee, Tzong-Huei;Ismail, Wael;Tsai, Ching-Yen;Lin, Ching-Wen;Tsai, Yu-Wen;Chiang, Yin-Ru
Contributors:	工學院環境工程研究所
Keywords:	Activation;Aerobic conditions;Alcohol use;Bacteria;Biodegradation;Biodiversity;Biology;Carbon;Cholesterol;Cholesterol - metabolism;Classical pathway;Cytochrome;Degradation;Gordonia;Hydroxylation;Intermediates;Isomerization;Metabolism;Mycobacterium tuberculosis;Oxygen;Oxygen - metabolism;Oxygenase;Oxygenases - metabolism;Rhodocyclaceae - metabolism;Steroids;Sterols;Studies;Substrates;Tuberculosis
Date:	2013-06-24
Issue Date:	2026-04-23 14:58:21 (UTC+8)
Publisher:	Public Library of Science;United States: Public Library of Science
Abstract:	摘要： Cholesterol is one of the most ubiquitous compounds in nature. The 9,10-seco-pathway for the aerobic degradation of cholesterol was established thirty years ago. This pathway is characterized by the extensive use of oxygen and oxygenases for substrate activation and ring fission. The classical pathway was the only catabolic pathway adopted by all studies on cholesterol-degrading bacteria. Sterolibacterium denitrificans can degrade cholesterol regardless of the presence of oxygen. Here, we aerobically grew the model organism with (13)C-labeled cholesterol, and substrate consumption and intermediate production were monitored over time. Based on the detected (13)C-labeled intermediates, this study proposes an alternative cholesterol catabolic pathway. This alternative pathway differs from the classical 9,10-seco-pathway in numerous important aspects. First, substrate activation proceeds through anaerobic C-25 hydroxylation and subsequent isomerization to form 26-hydroxycholest-4-en-3-one. Second, after the side chain degradation, the resulting androgen intermediate is activated by adding water to the C-1/C-2 double bond. Third, the cleavage of the core ring structure starts at the A-ring via a hydrolytic mechanism. The (18)O-incorporation experiments confirmed that water is the sole oxygen donor in this catabolic pathway. 其他題名： PLoS One 出版者： United States: Public Library of Science 出版日期： 2013-06-24 出處： PloS one, 2013-06, Vol.8 (6), p.e66675 資源來源： DOAJ Directory of Open Access Journals (WRLC) 版權： COPYRIGHT 2013 Public Library of Science 版權： 2013 Wang et?al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 版權： 2013 Wang et?al 2013 Wang et?al 識別號： ISSN: 1932-6203 識別號： EISSN: 1932-6203 識別號： DOI: 10.1371/journal.pone.0066675 識別號： PMID: 23826110
Appears in Collections:	[Graduate Institute of Environmental Engineering ] journal & Dissertation

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