Modeling catalytic promiscuity in the alkaline phosphatase superfamily.

ABSTRACT: In recent years, it has become increasingly clear that promiscuity plays a key role in the evolution of new enzyme function. This finding has helped to elucidate fundamental aspects of molecular evolution. While there has been extensive experimental work on enzyme promiscuity, computational modeling of the chemical details of such promiscuity has traditionally fallen behind the advances in experimental studies, not least due to the nearly prohibitive computational cost involved in examining multiple substrates with multiple potential mechanisms and binding modes in atomic detail with a reasonable degree of accuracy. However, recent advances in both computational methodologies and power have allowed us to reach a stage in the field where we can start to overcome this problem, and molecular

SUBMITTER: Duarte F 

PROVIDER: S-EPMC3693508 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature