Abstract The enzyme 2-deoxy- d -ribose-5-phosphate aldolase (DERA) is a useful tool for synthesizing statin side-chain intermediates. In this work, we identified the DERA from Streptococcus suis (SsDERA) by structural and sequence alignment and highly expressed it in Escherichia coli BL21. The recombinant SsDERA had a specific activity of 18.2 U mg−1, KM of 0.8 mM, and Vmax of 32.9 μmol min−1 mg−1 toward 2-deoxy- d -ribose-5-phosphate under the optimal conditions: 40 °C and pH 7.0. The enzyme retained 23.3 % activity after incubation in 200 mM acetaldehyde for 2 h and 58.2 % activity in 100 mM chloroacetaldehyde for 2 h. The enzyme showed moderate activity and aldehyde tolerance compared with reported DERAs. The SsDERA-catalyzed reaction between 200 mM acetaldehyde and 100 mM chloroacetaldehyde generated (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranose in 76 % yield in 8 h. This work provides a new DERA for the synthesis of (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranose, which is a potential candidate for the industrial synthesis of statin intermediates.

中文翻译：

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使用来自猪链球菌的新型2-脱氧-d-核糖-5-磷酸醛缩酶高效合成(3R,5S)-6-氯-2,4,6-三脱氧六吡喃糖，具有中等活性和醛耐受性

摘要 2-脱氧-d-核糖-5-磷酸醛缩酶（DERA）是合成他汀类药物侧链中间体的有用工具。在这项工作中，我们通过结构和序列比对鉴定了来自猪链球菌 (SsDERA) 的 DERA，并在大肠杆菌 BL21 中高度表达。重组SsDERA在最佳条件下对2-脱氧-d-核糖-5-磷酸的比活性为18.2 U mg-1，KM为0.8 mM，Vmax为32.9 μmol min-1 mg-1：40 °C和 pH 值 7.0。该酶在 200 mM 乙醛中孵育 2 小时后保留了 23.3% 的活性，在 100 mM 氯乙醛中孵育 2 小时后保留了 58.2% 的活性。与报道的 DERA 相比，该酶表现出中等活性和醛耐受性。SsDERA 催化 200 mM 乙醛和 100 mM 氯乙醛之间的反应生成 (3R,5S)-6-chloro-2,4，6-三脱氧六吡喃糖在 8 小时内的产率为 76%。该工作为(3R,5S)-6-氯-2,4,6-三脱氧六吡喃糖的合成提供了一种新的DERA，是他汀类中间体工业合成的潜在候选者。