The 3-hydroxypiperidine moiety is a privileged scaffold encountered in many bioactive compounds. An NADPH-dependent reductase (YGL039W) from Kluyveromyces marxianus ATCC 748 was isolated to show excellent catalytic activity in (R)-N-Boc-3-hydroxypiperidine [(R)-NBHP] production. Using a GDH-catalyzed cofactor-recycling system to ensure a sufficient supply of NADPH, the effects of temperature, pH, metal ions, substrate concentration, biocatalyst dosage, and cofactors on the YGL039W-catalyzed bioreduction were investigated and optimized. Finally, an extremely high concentration of N-Boc-piperidin-3-one (NBPO, 400 g/L) could be completely reduced to (R)-NBHP (> 99% ee), with a total turnover number of 20,000. This process shows significant potential for the industrial production of (R)-NBHP.

3-羟基哌啶部分是许多生物活性化合物中遇到的特有支架。分离自马克斯克鲁维酵母ATCC 748的NADPH依赖性还原酶（YGL039W）以显示出在（R）-N - Boc -3-羟基哌啶[（R）-NBHP]生产中的优异催化活性。使用GDH催化的辅助因子循环系统以确保提供足够的NADPH，研究并优化了温度，pH，金属离子，底物浓度，生物催化剂剂量和辅助因子对YGL039W催化的生物还原的影响。最后，极高浓度的N -Boc-哌啶-3-酮（NBPO，400 g / L）可以完全还原为（R）-NBHP（> 99％ee），总营业额为20,000。该方法显示出工业生产（R）-NBHP的巨大潜力。