Unknown

Dataset Information

0

Accelerating Enzymatic Catalysis Using Vortex Fluidics.


ABSTRACT: Enzymes catalyze chemical transformations with outstanding stereo- and regio-specificities, but many enzymes are limited by their long reaction times. A general method to accelerate enzymes using pressure waves contained within thin films is described. Each enzyme responds best to specific frequencies of pressure waves, and an acceleration landscape for each protein is reported. A vortex fluidic device introduces pressure waves that drive increased rate constants (kcat ) and enzymatic efficiency (kcat /Km ). Four enzymes displayed an average seven-fold acceleration, with deoxyribose-5-phosphate aldolase (DERA) achieving an average 15-fold enhancement using this approach. In solving a common problem in enzyme catalysis, a powerful, generalizable tool for enzyme acceleration has been uncovered. This research provides new insights into previously uncontrolled factors affecting enzyme function.

SUBMITTER: Britton J 

PROVIDER: S-EPMC5524626 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Accelerating Enzymatic Catalysis Using Vortex Fluidics.

Britton Joshua J   Meneghini Luz M LM   Raston Colin L CL   Weiss Gregory A GA  

Angewandte Chemie (International ed. in English) 20160805 38


Enzymes catalyze chemical transformations with outstanding stereo- and regio-specificities, but many enzymes are limited by their long reaction times. A general method to accelerate enzymes using pressure waves contained within thin films is described. Each enzyme responds best to specific frequencies of pressure waves, and an acceleration landscape for each protein is reported. A vortex fluidic device introduces pressure waves that drive increased rate constants (kcat ) and enzymatic efficiency  ...[more]

Similar Datasets

| S-EPMC6992170 | biostudies-literature
| S-EPMC5748167 | biostudies-literature
| S-EPMC4333057 | biostudies-other
| S-EPMC4839392 | biostudies-literature
| S-EPMC3625203 | biostudies-literature
| S-EPMC9292696 | biostudies-literature
| S-EPMC6396832 | biostudies-literature
| S-EPMC11336958 | biostudies-literature
| S-EPMC8297476 | biostudies-literature
| S-EPMC3907816 | biostudies-literature