Recently I am researching about THERMOANAEROBACTER-ETHANOLICUS; SATURATION MUTAGENESIS; MOLECULAR-DYNAMICS; DIRECTED EVOLUTION; SUBSTRATE-SPECIFICITY; ASYMMETRIC REDUCTION; BIOCATALYSIS; KETOREDUCTASE; MUTATION; ENZYME, Saw an article supported by the CAS Pioneer Hundred Talents Program [2016-053]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31700698, 21532008, 21676120, 21772142]; Key Research Program of the Chinese Academy of SciencesChinese Academy of Sciences [KFZD-SW-212]; Natural Science Foundation of TianjinNatural Science Foundation of Tianjin [18JCYBJC24600]; Open Project Funding of the State Key Laboratory of Bioreactor Engineering [2017OPEN02]; Key Projects in the Tianjin Science & Technology Pillar Program [15PTCYSY00020]; National Basic Research Program of China (973 Program)National Basic Research Program of China [2014CB745100]; Priority Academic Program Development of Jiangsu Higher Education Institutions; Top-notch Academic Programs Project of Jiangsu Higher Education Institutions; National First-Class Discipline Program of Light Industry Technology and Engineering [LITE2018-09]. Published in WILEY-V C H VERLAG GMBH in WEINHEIM ,Authors: Liu, BB; Qu, G; Li, JK; Fan, WC; Ma, JA; Xu, Y; Nie, Y; Sun, ZT. The CAS is 91-02-1. Through research, I have a further understanding and discovery of Phenyl(pyridin-2-yl)methanone. Category: pyridine-derivatives
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.
Category: pyridine-derivatives. Bye, fridends, I hope you can learn more about C12H9NO, If you have any questions, you can browse other blog as well. See you lster.
Reference:
Pyridine – Wikipedia,
,Pyridine | C5H5N – PubChem