Role of induced fit in enzyme specificity: a molecular forward/reverse switch.

ABSTRACT: Enzyme structures solved with and without bound substrate often show that substrate-induced conformational changes bring catalytic residues into alignment, alter the local environment, and position the substrate for catalysis. Although the structural data are compelling, the role of conformational changes in enzyme specificity has been controversial in that specificity is a kinetic property that is not easy to predict based upon structure alone. Recent studies on DNA polymerization have illuminated the role of substrate-induced conformational changes in enzyme specificity by showing that the rate at which the enzyme opens to release the bound substrate is a key kinetic parameter. The slow release of a correct substrate commits it to the forward reaction so that specificity is determined so

SUBMITTER: Johnson KA 

PROVIDER: S-EPMC2546551 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature