7emg
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Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+
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Structural highlights
FunctionA0A0G8B235_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 PubMedA 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
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This page was last modified 16:56, 29 November 2023.