Exploring functionally related enzymes using radially distributed properties of active sites around the reacting points of bound ligands.

ABSTRACT:

Background

Structural genomics approaches, particularly those solving the 3D structures of many proteins with unknown functions, have increased the desire for structure-based function predictions. However, prediction of enzyme function is difficult because one member of a superfamily may catalyze a different reaction than other members, whereas members of different superfamilies can catalyze the same reaction. In addition, conformational changes, mutations or the absence of a particular catalytic residue can prevent inference of the mechanism by which catalytic residues stabilize and promote the elementary reaction. A major hurdle for alignment-based methods for prediction of function is the absence (despite its importance) of a measure of similarity of the physicochemical properti

SUBMITTER: Ueno K 

PROVIDER: S-EPMC3408369 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature