Novel 7alpha-hydroxysteroid dehydrogenase gene S1-a-2

Abstract

The invention relates to hydroxysteroid dehydrogenase, in particular to a novel 7alpha-hydroxysteroid dehydrogenase gene S1-a-2. A nucleotide sequence of the gene is shown as SEQ ID NO.2. A novel 7alpha-hydroxysteroid dehydrogenase with an amino acid sequence shown as SEQ ID NO.1 is coded and is capable of catalyzing CDCA (chenodeoxycholic acid) and TCDCA (taurochenodeoxycholic acid) to generate 7K-LCA (7-ketone lithocholic acid) and T7K-LCA (tauro-7-keto lithocholic acid), catalytic activity of the novel 7alpha-hydroxysteroid dehydrogenase for the CDCA or TCDCA is about twice of that of Clostridium sardiniense 7alpha-HSDH for the same, and accordingly the novel 7alpha-hydroxysteroid dehydrogenase is high in industrial application value.

Description

technical field

[0001] The invention relates to hydroxysteroid dehydrogenase, in particular to a novel 7α-hydroxysteroid dehydrogenase gene S1-a-2. Background technique

[0002] The asymmetric reduction of carbonyl groups has always been one of the hotspots in chemical reaction research. Although the current chemical methods have achieved certain results, they often have disadvantages such as limited types and numbers of catalysts, low stereoselectivity, expensive auxiliary reagents, and difficult recovery. The enzymatic reaction not only has high efficiency, chemoselectivity, regioselectivity but also high stereoselectivity. The enzymatic reaction mediated by hydroxysteroid dehydrogenase (Hydroxysteroid dehydrogenase, HSDH) has relatively strict stereoselectivity and "not" strict substrate specificity. For example, as early as the early 1980s, scientists have begun to use 7α-, 7β-HSDH produced by microorganisms to combine epimerization with chenodeoxycholic acid (Chenodeo...

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