The active site of a carbohydrate esterase displays divergent catalytic and noncatalytic binding functions.

ABSTRACT: Multifunctional proteins, which play a critical role in many biological processes, have typically evolved through the recruitment of different domains that have the required functional diversity. Thus the different activities displayed by these proteins are mediated by spatially distinct domains, consistent with the specific chemical requirements of each activity. Indeed, current evolutionary theory argues that the colocalization of diverse activities within an enzyme is likely to be a rare event, because it would compromise the existing activity of the protein. In contrast to this view, a potential example of multifunctional recruitment into a single protein domain is provided by CtCel5C-CE2, which contains an N-terminal module that displays cellulase activity and a C-terminal module, CtC

SUBMITTER: Montanier C 

PROVIDER: S-EPMC2661963 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature