| Identification and characterization of two bile acid coenzyme A transferases from clostridium scindens, a bile acid 7{alpha}-dehydroxylating intestinal bacterium. | |
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MedLine Citation:
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PMID: 22021638 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The human bile acid pool composition is composed of both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid). Secondary bile acids are formed by the 7α-dehydroxylation of primary bile acids carried out by intestinal anaerobic bacteria. We have previously described a multi-step biochemical pathway in Clostridium scindens that is responsible for bile acid 7α-dehydroxylation. We have identified a large (12 kb) bile acid inducible (bai) operon in this bacterium that encodes eight genes involved in bile acid 7α-dehydroxylation. However, the function of the baiF gene product in this operon has not been elucidated. In the current study, we cloned and expressed the baiF gene in E. coli and discovered it has bile acid coenzyme A (CoA) transferase activity. In addition, we also discovered a second bai operon encoding three genes. The baiK gene in this operon was expressed in E. coli and found to encode a second bile acid Co A transferase. Both bile acid CoA transferases were determined to be members of the type III family by amino acid sequence comparisons. Both bile acid CoA transferases had broad substrate specificity, except the baiK gene product, which failed to use lithocholyl-CoA as a CoA donor. A model is presented showing the possible function of bile acid CoA transferases in the 7α-dehyhdroxylation pathway. |
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Authors:
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Jason M Ridlon; Phillip B Hylemon |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-20 |
Journal Detail:
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Title: Journal of lipid research Volume: - ISSN: 0022-2275 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-24 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0376606 Medline TA: J Lipid Res Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Virginia Commonwealth University, United States. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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