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Effects of Macromolecular Crowding on Alcohol Dehydrogenase and Citrate Synthase Kinetics
Author(s) -
Slade Kristin,
Chung Charmaine,
Jackson Jasmine
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.lb217
Subject(s) - kinetics , macromolecular crowding , alcohol dehydrogenase , chemistry , macromolecule , dextran , citrate synthase , enzyme , biochemistry , crowding , biophysics , enzyme kinetics , biology , active site , physics , quantum mechanics , neuroscience
Most of our understanding of enzyme kinetics is based on experiments conducted in dilute solution. However, these conditions do not accurately represent the crowded cellular environment, which contains high concentrations (300–400g/L) of various macromolecules such as proteins, carbohydrates and ribosomes. This crowding reduces the volume of solvent available for other molecules in the solution and has previously been shown to impact the behavior of enzymes. To study these potential consequences, the Michaelis‐Menten kinetics of yeast alcohol dehydrogenase (YADH) and citrate synthase (CS) were monitored under crowded conditions. Spectroscopic assays were performed in the presence and absence of high concentrations of dextran or glucose, the small‐molecule counterpart. This study also explored the effects of mixed crowding by combining equal ratios of different sizes of dextran. Overall, the effects of crowding depend on the size and concentration of the crowding agent. Furthermore, the results demonstrated that, in addition to merely excluded volume effects, chemical interactions from crowders must also be considered. Support or Funding Information Camille and Henry Drefyus Foundation. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .