新型无外加辅因子还原酶以高时空产率高效合成血管紧张素转化酶（ACE）抑制剂手性前体。
Efficient synthesis of a chiral precursor for angiotensin-converting enzyme (ACE) inhibitors in high space-time yield by a new reductase without external cofactors.
机构信息
Laboratory of Biocatalysis and Synthetic Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, People's Republic of China.
出版信息
Org Lett. 2012 Apr 20;14(8):1982-5. doi: 10.1021/ol300397d. Epub 2012 Apr 5.
A new reductase, CgKR2, with the ability to reduce ethyl 2-oxo-4-phenylbutyrate (OPBE) to ethyl (R)-2-hydroxy-4-phenylbutyrate ((R)-HPBE), an important chiral precursor for angiotensin-converting enzyme (ACE) inhibitors, was discovered. For the first time, (R)-HPBE with >99% ee was produced via bioreduction of OPBE at 1 M without external addition of cofactors. The space-time yield (700 g·L(-1)·d(-1)) was 27 times higher than the highest record.
一种新的还原酶 CgKR2 被发现，它能够将乙基 2-氧代-4-苯基丁酸酯 (OPBE) 还原为(R)-2-羟基-4-苯基丁酸乙酯 ((R)-HPBE)，(R)-HPBE 是血管紧张素转换酶 (ACE) 抑制剂的重要手性前体。首次在无需外加辅因子的情况下，在 1 M 下通过 OPBE 的生物还原反应生产出 ee 值大于 99%的 (R)-HPBE。时空产率（700 g·L(-1)·d(-1)）比最高记录高出 27 倍。
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