7emg | pdb_00007emg

Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+

spinqualitylabelsall models 7emg, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7emg is a 2 chain structure with sequence from Serratia marcescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.449Å Ligands: EDO, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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