Cytosol-Mimetic Chemistry: Kinetics of the Trypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate upon Addition of Polyethylene Glycol and N-tert-Butyl Acetoacetamide
| Autor: | Nabil Asaad, Jan B. F. N. Engberts |
|---|---|
| Přispěvatelé: | Faculty of Science and Engineering |
| Rok vydání: | 2003 |
| Předmět: |
ORGANIC-SOLVENTS
PROTEINS Biochemistry Catalysis Acetoacetates Polyethylene Glycols Enzyme catalysis Nitrophenols Chemical kinetics Hydrolysis Cytosol Colloid and Surface Chemistry Reaction rate constant Biomimetic Materials WATER Organic chemistry Trypsin GeneralLiterature_REFERENCE(e.g. dictionaries encyclopedias glossaries) chemistry.chemical_classification Aqueous solution Chemistry Substrate (chemistry) General Chemistry Amides Kinetics Enzyme ComputingMethodologies_DOCUMENTANDTEXTPROCESSING |
| Zdroj: | Journal of the American Chemical Society, 125(23), 6874-6875. AMER CHEMICAL SOC |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja034298f |
| Popis: | The sensitivity of an enzyme to its environment has provoked much interest both for its immediate relevance to biochemistry and for the use of enzymes in chemical synthesis. The intercellular or extracellular environment in which an enzyme naturally operates is crowded with macromolecular, small-molecule, and ionic solutes and hence is markedly different from the dilute aqueous buffer solutions commonly cited for comparisons of biochemical processes. We report the results of a kinetic study into the effects of such a crowded solution on the rate of an enzyme-mediated process-the trypsin-catalyzed hydrolysis of a nonnatural substrate ester. The catalytic rate constant decreases linearly with solvent polarity, but substrate binding is independent of the concentration of added crowding agent up to 395 g/L. |
| Databáze: | OpenAIRE |
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