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1

An unexplored pathway for degradation of cholate requires a 7α-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp. strain Chol11.

Yücel O, Drees S, Jagmann N, Patschkowski T, Philipp B. Yücel O, et al. Environ Microbiol. 2016 Dec;18(12):5187-5203. doi: 10.1111/1462-2920.13534. Epub 2016 Nov 13. Environ Microbiol. 2016. PMID: 27648822

2

A Novel Steroid-Coenzyme A Ligase from Novosphingobium sp. Strain Chol11 Is Essential for an Alternative Degradation Pathway for Bile Salts.

Yücel O, Holert J, Ludwig KC, Thierbach S, Philipp B. Yücel O, et al. Appl Environ Microbiol. 2017 Dec 15;84(1):e01492-17. doi: 10.1128/AEM.01492-17. Print 2018 Jan 1. Appl Environ Microbiol. 2017. PMID: 29054875 Free PMC article.

3

The 7α-hydroxysteroid dehydratase Hsh2 is essential for anaerobic degradation of the steroid skeleton of 7α-hydroxyl bile salts in the novel denitrifying bacterium Azoarcus sp. strain Aa7.

Yücel O, Borgert SR, Poehlein A, Niermann K, Philipp B. Yücel O, et al. Environ Microbiol. 2019 Feb;21(2):800-813. doi: 10.1111/1462-2920.14508. Epub 2019 Jan 24. Environ Microbiol. 2019. PMID: 30680854

4

Evidence of distinct pathways for bacterial degradation of the steroid compound cholate suggests the potential for metabolic interactions by interspecies cross-feeding.

Holert J, Yücel O, Suvekbala V, Kulić Z, Möller H, Philipp B. Holert J, et al. Environ Microbiol. 2014 May;16(5):1424-40. doi: 10.1111/1462-2920.12407. Epub 2014 Feb 24. Environ Microbiol. 2014. PMID: 24447610

5

Comparative Analysis of Bile-Salt Degradation in Sphingobium sp. Strain Chol11 and Pseudomonas stutzeri Strain Chol1 Reveals Functional Diversity of Proteobacterial Steroid Degradation Enzymes and Suggests a Novel Pathway for Side Chain Degradation.

Feller FM, Richtsmeier P, Wege M, Philipp B. Feller FM, et al. Appl Environ Microbiol. 2021 Oct 28;87(22):e0145321. doi: 10.1128/AEM.01453-21. Epub 2021 Sep 1. Appl Environ Microbiol. 2021. PMID: 34469190 Free PMC article.

6

Proteome, Bioinformatic, and Functional Analyses Reveal a Distinct and Conserved Metabolic Pathway for Bile Salt Degradation in the Sphingomonadaceae.

Feller FM, Wöhlbrand L, Holert J, Schnaars V, Elsner L, Mohn WW, Rabus R, Philipp B. Feller FM, et al. Appl Environ Microbiol. 2021 Sep 10;87(19):e0098721. doi: 10.1128/AEM.00987-21. Epub 2021 Sep 10. Appl Environ Microbiol. 2021. PMID: 34260303 Free PMC article.

7

Identification of bypass reactions leading to the formation of one central steroid degradation intermediate in metabolism of different bile salts in Pseudomonas sp. strain Chol1.

Holert J, Yücel O, Jagmann N, Prestel A, Möller HM, Philipp B. Holert J, et al. Environ Microbiol. 2016 Oct;18(10):3373-3389. doi: 10.1111/1462-2920.13192. Epub 2016 Feb 4. Environ Microbiol. 2016. PMID: 26691005

8

Biochemical and genetic investigation of initial reactions in aerobic degradation of the bile acid cholate in Pseudomonas sp. strain Chol1.

Birkenmaier A, Holert J, Erdbrink H, Moeller HM, Friemel A, Schoenenberger R, Suter MJ, Klebensberger J, Philipp B. Birkenmaier A, et al. J Bacteriol. 2007 Oct;189(20):7165-73. doi: 10.1128/JB.00665-07. Epub 2007 Aug 10. J Bacteriol. 2007. PMID: 17693490 Free PMC article.

9

Investigations on the Degradation of the Bile Salt Cholate via the 9,10-Seco-Pathway Reveals the Formation of a Novel Recalcitrant Steroid Compound by a Side Reaction in Sphingobium sp. Strain Chol11.

Feller FM, Eilebrecht S, Nedielkov R, Yücel O, Alvincz J, Salinas G, Ludwig KC, Möller H, Philipp B. Feller FM, et al. Microorganisms. 2021 Oct 14;9(10):2146. doi: 10.3390/microorganisms9102146. Microorganisms. 2021. PMID: 34683472 Free PMC article.

10

Identification of a thiolase gene essential for β-oxidation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1.

Birkenmaier A, Möller HM, Philipp B. Birkenmaier A, et al. FEMS Microbiol Lett. 2011 May;318(2):123-30. doi: 10.1111/j.1574-6968.2011.02250.x. Epub 2011 Mar 8. FEMS Microbiol Lett. 2011. PMID: 21362022

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