Shuffling Active Site Substate Populations Affects Catalytic Activity: The Case of Glucose Oxidase.

ABSTRACT: Glucose oxidase has wide applications in the pharmaceutical, chemical, and food industries. Many recent studies have enhanced key properties of this enzyme using directed evolution, yet without being able to reveal why these mutations are actually beneficial. This work presents a synergistic combination of experimental and computational methods, indicating how mutations, even when distant from the active site, positively affect glucose oxidase catalysis. We have determined the crystal structures of glucose oxidase mutants containing molecular oxygen in the active site. The catalytically important His516 residue has been previously shown to be flexible in the wild-type enzyme. The molecular dynamics simulations performed in this work allow us to quantify this floppiness, revealing that His5

SUBMITTER: Petrovic D 

PROVIDER: S-EPMC5745072 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature