Probing of b-galactosidases with galactonoamidines reveals importance of active site loops.
by Pickens, Jessica B.; Striegler, Susanne
Glycoside hydrolases are one of the most catalytically efficient enzymes known. In order to understand the catalytic capabilities of these enzymes, galactonoamidines with various aglycons were developed. The interactions of these galactonoamidines within the active site of glycoside hydrolases were examd. through kinetic evaluation, mol. docking, and mol. dynamics. These evaluations revealed that the binding of the galactonoamidines within the active sites of b-galactosidases from fungal (A. oryzae), bacterial (E. coli), and mammalian (bovine liver) sources initiates an induced fit conformation.