Basso, Alessandra; Braiuca, Paolo; Ebert, Cynthia; Gardossi, Lucia; Linda, Paolo; Benedetti, Fabio published the artcile< GRID/tetrahedral intermediate computational approach to the study of selectivity of penicillin G acylase in amide bond synthesis>, Safety of Methyl 2-(2-nitrophenyl)acetate, the main research area is penicillin G acylase selectivity active site tetrahedral intermediate.
Mol. modeling was used to investigate the catalytic site of penicillin G acylase (PGA) by building up a simple enzyme-ligand model able to describe and predict the enzyme selectivity. The investigation was based on a double computational approach: first, the GRID computational procedure was applied to gain a qual. description of the chem. features of the PGA active site; second, a classical “”transition state approach”” was used to simulate the tetrahedral intermediates and to evaluate their energies. GRID calculations employed different probes which gave a complete description of the chem. interactions occurring upon binding of different ligands, thus indicating those structures having good affinity with the active site of the enzyme. Tetrahedral intermediates were constructed on the basis of GRID results and provided both geometrical features and energies of enzyme-substrate interaction. Such energies were compared to exptl. kinetic data obtained in the enzymic acylation of L-phenylglycine Me ester using various Me phenylacetate derivatives The good agreement of computational results with exptl. evidence demonstrates the validity of the model as a rapid and flexible tool to describe and predict the enzyme selectivity.
Biochimica et Biophysica Acta, Proteins and Proteomics published new progress about Enzyme functional sites, active. 30095-98-8 belongs to class esters-buliding-blocks, and the molecular formula is C9H9NO4, Safety of Methyl 2-(2-nitrophenyl)acetate.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics