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

Yuecel O, Drees S, Jagmann N, Patschkowski T, Philipp B (2016)
ENVIRONMENTAL MICROBIOLOGY 18(12): 5187-5203.

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Bile salts such as cholate are surface-active steroid compounds with functions for digestion and signaling in vertebrates. Upon excretion into soil and water bile salts are an electron-and carbon-rich growth substrate for environmental bacteria. Degradation of bile salts proceeds via intermediates with a 3-keto-Delta(1,4)-diene structure of the steroid skeleton as shown for e.g. Pseudomonas spp. Recently, we isolated bacteria degrading cholate via intermediates with a 3-keto-7-deoxy-Delta(4,6)-structure of the steroid skeleton suggesting the existence of a second pathway for cholate degradation. This potential new pathway was investigated with Novosphingobium sp. strain Chol11. A 7 alpha-hydroxysteroid dehydratase encoded by hsh2 was identified, which was required for the formation of 3-keto-7-deoxy-Delta(4,6)-metabolites. A hsh2 deletion mutant could still grow with cholate but showed impaired growth. Cholate degradation of this mutant proceeded via 3-keto-Delta(1,4)-diene metabolites. Heterologous expression of Hsh2 in the bile salt-degrading Pseudomonas sp. strain Chol1 led to the formation of a dead-end steroid with a 3-keto-7-deoxy-Delta(4,6)-diene structure. Hsh2 is the first steroid dehydratase with an important function in a metabolic pathway of bacteria that use bile salts as growth substrates. This pathway contributes to a broad metabolic repertoire of Novosphingobium strain Chol11 that may be advantageous in competition with other bile salt-degrading bacteria.
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Yuecel O, Drees S, Jagmann N, Patschkowski T, Philipp B. An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11. ENVIRONMENTAL MICROBIOLOGY. 2016;18(12):5187-5203.
Yuecel, O., Drees, S., Jagmann, N., Patschkowski, T., & Philipp, B. (2016). An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11. ENVIRONMENTAL MICROBIOLOGY, 18(12), 5187-5203. doi:10.1111/1462-2920.13534
Yuecel, O., Drees, S., Jagmann, N., Patschkowski, T., and Philipp, B. (2016). An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11. ENVIRONMENTAL MICROBIOLOGY 18, 5187-5203.
Yuecel, O., et al., 2016. An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11. ENVIRONMENTAL MICROBIOLOGY, 18(12), p 5187-5203.
O. Yuecel, et al., “An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11”, ENVIRONMENTAL MICROBIOLOGY, vol. 18, 2016, pp. 5187-5203.
Yuecel, O., Drees, S., Jagmann, N., Patschkowski, T., Philipp, B.: An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11. ENVIRONMENTAL MICROBIOLOGY. 18, 5187-5203 (2016).
Yuecel, Onur, Drees, Steffen, Jagmann, Nina, Patschkowski, Thomas, and Philipp, Bodo. “An unexplored pathway for degradation of cholate requires a 7 alpha-hydroxysteroid dehydratase and contributes to a broad metabolic repertoire for the utilization of bile salts in Novosphingobium sp strain Chol11”. ENVIRONMENTAL MICROBIOLOGY 18.12 (2016): 5187-5203.
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