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The kinetics and mechanism of glycoside bond hydrolysis in the active center of β-galactosidase from escherichia coli

An acid-base mechanism for glycoside bond hydrolysis by β-galactosidase including the formation of two intermediate enzyme-substrate complexes ES1 and ES2 with two bond redistribution chains is suggested. A kinetic analysis was performed using a three-step kinetic scheme including the formation of glycosylated enzyme (E-Gal). This allowed us to calculate the elementary kinetic constants k 2 , k 3 , and K S for the reaction with o-nitrophenyl-β-D-galactopyranoside as a model substrate.