Substrate-driven chemotactic assembly in an enzyme cascade
| Autor: | Stephen J. Benkovic, Henri Palacci, Xi Zhao, Vinita Yadav, Peter J. Butler, Ayusman Sen, Michelle M. Spiering, Michael K. Gilson, Henry Hess |
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| Rok vydání: | 2017 |
| Předmět: |
General Chemical Engineering
02 engineering and technology 010402 general chemistry 01 natural sciences Substrate Specificity Fructose-Bisphosphate Aldolase Hexokinase Glycolysis chemistry.chemical_classification Molecular Structure Chemotaxis Glucose-6-Phosphate Isomerase Substrate (chemistry) General Chemistry 021001 nanoscience & nanotechnology 0104 chemical sciences Metabolic pathway Enzyme Phosphofructokinases chemistry Cascade Biocatalysis Biophysics Substrate specificity 0210 nano-technology |
| Zdroj: | Nature Chemistry. 10:311-317 |
| ISSN: | 1755-4349 1755-4330 |
| DOI: | 10.1038/nchem.2905 |
| Popis: | Enzymatic catalysis is essential to cell survival. In many instances, enzymes that participate in reaction cascades have been shown to assemble into metabolons in response to the presence of the substrate for the first enzyme. However, what triggers metabolon formation has remained an open question. Through a combination of theory and experiments, we show that enzymes in a cascade can assemble via chemotaxis. We apply microfluidic and fluorescent spectroscopy techniques to study the coordinated movement of the first four enzymes of the glycolysis cascade: hexokinase, phosphoglucose isomerase, phosphofructokinase and aldolase. We show that each enzyme independently follows its own specific substrate gradient, which in turn is produced by the preceding enzymatic reaction. Furthermore, we find that the chemotactic assembly of enzymes occurs even under cytosolic crowding conditions. |
| Databáze: | OpenAIRE |
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