A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues.

ABSTRACT: The ability of an enzyme to select and act upon a specific class of compounds with unerring precision and efficiency is an essential feature of life. Simultaneously, these enzymes often catalyze the reaction of a range of similar substrates of the same class, and also have promiscuous activities on unrelated substrates. Previously, we have established a methodology to quantify promiscuous activities in a wide range of proteins. In the current work, we quantitatively characterize the active site for the ability to catalyze distinct, yet related, substrates (BRASS). A protein with known structure and active site residues provides the framework for computing 'duplicate' residues, each of which results in slightly modified replicas of the active site scaffold. Such spatial congruence is supple

SUBMITTER: Chakraborty S 

PROVIDER: S-EPMC3500292 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature