Resolution of Submillisecond Kinetics of Multiple Reaction Pathways for Lactate Dehydrogenase.

ABSTRACT: Enzymes are known to exhibit conformational flexibility. An important consequence of this flexibility is that the same enzyme reaction can occur via multiple reaction pathways on a reaction landscape. A model enzyme for the study of reaction landscapes is lactate dehydrogenase. We have previously used temperature-jump (T-jump) methods to demonstrate that the reaction landscape of lactate dehydrogenase branches at multiple points creating pathways with varied reactivity. A limitation of this previous work is that the T-jump method makes only small perturbations to equilibrium and may not report conclusively on all steps in a reaction. Therefore, interpreting T-jump results of lactate dehydrogenase kinetics has required extensive computational modeling work. Rapid mixing methods offer a comp

SUBMITTER: Reddish MJ 

PROVIDER: S-EPMC5425397 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature