Ontology highlight
ABSTRACT:
SUBMITTER: Lu J
PROVIDER: S-EPMC9589722 | biostudies-literature | 2022 Oct
REPOSITORIES: biostudies-literature
Lu Jiajun J Scheerer David D Haran Gilad G Li Wenfei W Wang Wei W
The journal of physical chemistry. B 20221012 41
The catalytic cycle of the enzyme adenylate kinase involves large conformational motions between open and closed states. A previous single-molecule experiment showed that substrate binding tends to accelerate both the opening and the closing rates and that a single turnover event often involves multiple rounds of conformational switching. In this work, we showed that the repeated conformational transitions of adenylate kinase are essential for the relaxation of incorrectly bound substrates into ...[more]