The role of ligand-gated conformational changes in enzyme catalysis

• Type: Article in International Scientific Journal
• Date: 2019

Authors

Moreira, C (Author) Other; Calixto, AR (Author) Other; Richard, JP (Author) Other; Kamerlin, SCL (Author) Other

Journal

Title: Biochemical Society Transactions

Vol. 47

Pages: 1449-1460

ISSN: 0300-5127

Publisher: PORTLAND PRESS LTD

Other information

Authenticus ID: P-00Y-72X

DOI: 10.1042/bst20190298

Abstract (EN): <jats:title>Abstract</jats:title> <jats:p>Structural and biochemical studies on diverse enzymes have highlighted the importance of ligand-gated conformational changes in enzyme catalysis, where the intrinsic binding energy of the common phosphoryl group of their substrates is used to drive energetically unfavorable conformational changes in catalytic loops, from inactive open to catalytically competent closed conformations. However, computational studies have historically been unable to capture the activating role of these conformational changes. Here, we discuss recent experimental and computational studies, which can remarkably pinpoint the role of ligand-gated conformational changes in enzyme catalysis, even when not modeling the loop dynamics explicitly. Finally, through our joint analyses of these data, we demonstrate how the synergy between theory and experiment is crucial for furthering our understanding of enzyme catalysis.</jats:p>

Language: English

Type (Professor's evaluation): Scientific