Zhu, Dunming published the artcileHow carbonyl reductases control stereoselectivity: approaching the goal of rational design, Related Products of esters-buliding-blocks, the publication is Pure and Applied Chemistry (2010), 82(1), 117-128, database is CAplus.
Although Prelog’s rule and two hydrophobic binding pockets model have been used to predict and explain the stereoselectivity of enzymic ketone reduction, the mol. basis of stereo-recognition by carbonyl reductases has not been well understood. The stereo-selectivity is not only determined by the structures of enzymes and substrates, but also affected by the reaction conditions such as temperature and reaction medium. Structural anal. coupled with site-directed mutagenesis of stereo-complementary carbonyl reductases readily reveals the key elements of controlling stereo-selectivity in these enzymes. Enzyme-substrate docking and mol. modeling have been engaged to understand the enantio-selectivity diversity of the carbonyl reductase from Sporobolomyces salmonicolor (SSCR), and to guide site-saturation mutagenesis for altering the enantioselectivity of this enzyme. These studies provide valuable information for understanding of how the residues involved in substrate binding affect the orientation of bound substrate, and thus control the reaction stereo-selectivity. The in silico docking-guided semi-rational approach should be a useful methodol. for discovery of new carbonyl reductases.
Pure and Applied Chemistry published new progress about 350-19-6. 350-19-6 belongs to esters-buliding-blocks, auxiliary class Fluoride,Benzene,Ester, name is Ethyl 3,5-difluorobenzoate, and the molecular formula is C42H63O3P, Related Products of esters-buliding-blocks.
Referemce:
https://en.wikipedia.org/wiki/Ester,
Ester – an overview | ScienceDirect Topics