Single-Molecule Mechanistic Study of Enzyme Hysteresis

Yu Jiang, Xiang Li, Barrett R. Morrow, Arti Pothukuchy, Jimmy Gollihar, Richard Novak, Charles B. Reilly, Andrew D. Ellington, David R. Walt

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Hysteresis is an important feature of enzyme-catalyzed reactions, as it reflects the influence of enzyme regulation in the presence of ligands such as substrates or allosteric molecules. In typical kinetic studies of enzyme activity, hysteretic behavior is observed as a "lag" or "burst" in the time course of the catalyzed reaction. These lags and bursts are due to the relatively slow transition from one state to another state of the enzyme molecule, with different states having different kinetic properties. However, it is difficult to understand the underlying mechanism of hysteresis by observing bulk reactions because the different enzyme molecules in the population behave stochastically. In this work, we studied the hysteretic behavior of mutant β-glucuronidase (GUS) using a high-throughput single-molecule array platform and investigated the effect of thermal treatment on the hysteresis.

Original languageEnglish (US)
Pages (from-to)1691-1698
Number of pages8
JournalACS Central Science
Volume5
Issue number10
DOIs
StatePublished - Oct 23 2019

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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