Journal
PROTEIN SCIENCE
Volume 28, Issue 5, Pages 910-919Publisher
WILEY
DOI: 10.1002/pro.3599
Keywords
acidophilic; 7 alpha-hydroxysteroid dehydrogenase; short-chain dehydrogenases; reductases; bile acids
Categories
Funding
- Major New Drugs Innovation and Development [2017ZX09309006-003]
- Fundamental Research Funds for the Central Universities of China [106112017CDJXY230003]
- Fundamental Research Funds for the Central Universities [2018CDPTCG0001/37]
- National Science and Technology Major Projects [2017ZX09309006-003]
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7 alpha-Hydroxysteroid dehydrogenase (7 alpha-HSDH) is an NAD(P)H-dependent oxidoreductase belonging to the short-chain dehydrogenases/reductases. In vitro, 7 alpha-HSDH is involved in the efficient biotransformation of taurochenodeoxycholic acid (TCDCA) to tauroursodeoxycholic acid (TUDCA). In this study, a gene encoding novel 7 alpha-HSDH (named as St-2-1) from fecal samples of black bear was cloned and heterologously expressed in Escherichia coli. The protein has subunits of 28.3 kDa and a native size of 56.6 kDa, which suggested a homodimer. We studied the relevant properties of the enzyme, including the optimum pH, optimum temperature, thermal stability, activators, and inhibitors. Interestingly, the data showed that St-2-1 differs from the 7 alpha-HSDHs reported in the literature, as it functions under acidic conditions. The enzyme displayed its optimal activity at pH 5.5 (TCDCA). The acidophilic nature of 7 alpha-HSDH expands its application environment and the natural enzyme bank of HSDHs, providing a promising candidate enzyme for the biosynthesis of TUDCA or other related chemical entities.
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