In 2019 ADV SYNTH CATAL published article about THERMOANAEROBACTER-ETHANOLICUS; SATURATION MUTAGENESIS; MOLECULAR-DYNAMICS; DIRECTED EVOLUTION; SUBSTRATE-SPECIFICITY; ASYMMETRIC REDUCTION; BIOCATALYSIS; KETOREDUCTASE; MUTATION; ENZYME in [Liu, Beibei; Xu, Yan; Nie, Yao] Jiangnan Univ, Sch Biotechnol, Key Lab Ind Biotechnol, Minist Educ, Wuxi 214122, Jiangsu, Peoples R China; [Liu, Beibei; Qu, Ge; Li, Jun-Kuan; Fan, Wenchao; Sun, Zhoutong] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin Airport Econ Area, 32 West 7th Ave, Tianjin 300308, Peoples R China; [Li, Jun-Kuan; Ma, Jun-An] Tianjin Univ, Tianjin Key Lab Mol Optoelect Sci, Dept Chem, Tianjin 300072, Peoples R China; [Li, Jun-Kuan; Ma, Jun-An] Tianjin Univ, Tianjin Collaborat Innovat Ctr Chem Sci & Engn, Tianjin 300072, Peoples R China in 2019, Cited 82. The Name is Phenyl(pyridin-2-yl)methanone. Through research, I have a further understanding and discovery of 91-02-1. Recommanded Product: Phenyl(pyridin-2-yl)methanone
Directed evolution of enzymes for the asymmetric reduction of prochiral ketones to produce enantio-pure secondary alcohols is particularly attractive in organic synthesis. Loops located at the active pocket of enzymes often participate in conformational changes required to fine-tune residues for substrate binding and catalysis. It is therefore of great interest to control the substrate specificity and stereochemistry of enzymatic reactions by manipulating the conformational dynamics. Herein, a secondary alcohol dehydrogenase was chosen to enantioselectively catalyze the transformation of difficult-to-reduce bulky ketones, which are not accepted by the wildtype enzyme. Guided by previous work and particularly by structural analysis and molecular dynamics (MD) simulations, two key residues alanine 85 (A85) and isoleucine 86 (I86) situated at the binding pocket were thought to increase the fluctuation of a loop region, thereby yielding a larger volume of the binding pocket to accommodate bulky substrates. Subsequently, site-directed saturation mutagenesis was performed at the two sites. The best mutant, where residue alanine 85 was mutated to glycine and isoleucine 86 to leucine (A85G/I86L), can efficiently reduce bulky ketones to the corresponding pharmaceutically interesting alcohols with high enantioselectivities (similar to 99% ee). Taken together, this study demonstrates that introducing appropriate mutations at key residues can induce a higher flexibility of the active site loop, resulting in the improvement of substrate specificity and enantioselectivity.
Welcome to talk about 91-02-1, If you have any questions, you can contact Liu, BB; Qu, G; Li, JK; Fan, WC; Ma, JA; Xu, Y; Nie, Y; Sun, ZT or send Email.. Recommanded Product: Phenyl(pyridin-2-yl)methanone
Reference:
Pyridine – Wikipedia,
,Pyridine | C5H5N – PubChem