Structural highlights
Function
[A0A0G8B235_SERMA] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[ARBA:ARBA00002607][RuleBase:RU366074]
Publication Abstract from PubMed
A carbonyl reductase variant, SmCRM5, from Serratia marcescens was obtained through structure-guided directed evolution. The variant showed improved specific activity (U mg(-1)) towards most of the 16 tested substrates and gave high stereoselectivities of up to 99% in the asymmetric synthesis of 13 gamma-/delta-lactones. In particular, SmCRM5 showed a 13.8-fold higher specific activity towards the model substrate, i.e., 5-oxodecanoic acid, and gave (R)-delta-decalactone in 99% ee with a space-time yield (STY) of 301 g L(-1) d(-1). The preparative synthesis of six delta-lactones in high yields and with high enantiopurities showed the feasibility of the biocatalytic synthesis of these high-value-added chemicals, providing a cost-effective and green alternative to noble-metal catalysis.
Stereoselective synthesis of chiral delta-lactones via an engineered carbonyl reductase.,Wang T, Zhang XY, Zheng YC, Bai YP Chem Commun (Camb). 2021 Sep 24. doi: 10.1039/d1cc04542c. PMID:34559867[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang T, Zhang XY, Zheng YC, Bai YP. Stereoselective synthesis of chiral delta-lactones via an engineered carbonyl reductase. Chem Commun (Camb). 2021 Sep 24. doi: 10.1039/d1cc04542c. PMID:34559867 doi:http://dx.doi.org/10.1039/d1cc04542c
