Cytosol-mimetic chemistry: kinetics of the trypsin-catalyzed hydrolysis of p-nitrophenyl acetate upon addition of polyethylene glycol and N-tert-butyl acetoacetamide

Journal of the American Chemical Society
Nabil Asaad, Jan B F N Engberts

Abstract

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.

References

Sep 7, 1993·Biochemistry·G D Dzingeleski, R Wolfenden
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Feb 14, 2002·Trends in Biochemical Sciences·Alan S Verkman

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Citations

Dec 5, 2013·Biophysical Chemistry·Isabel PastorFrancesc Mas
Apr 27, 2005·Chemical Society Reviews·Mike J BlandamerJoao Carlos R Reis
Sep 20, 2008·Organic & Biomolecular Chemistry·Seung-kee Seo, Alexander Wei
Dec 17, 2014·International Journal of Molecular Sciences·Irina M KuznetsovaVladimir N Uversky
May 12, 2015·Biochimica Et Biophysica Acta·Shruti MittalLaishram Rajendrakumar Singh
Oct 4, 2017·Protein Science : a Publication of the Protein Society·Luis C AcostaAnnelise H Gorensek-Benitez
Aug 27, 2004·Biotechnology and Bioengineering·R SchoevaartR A Sheldon
Jun 6, 2014·Lab on a Chip·Vinay PagayAbraham D Stroock
Feb 5, 2019·Biochemistry·Shuntaro TakahashiNaoki Sugimoto

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