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Issue 48, 2013
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The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme

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Abstract

Recent work on a computationally-designed retroaldolase RA-61 suggested that most of the rate-acceleration brought about by this enzyme was due to non-specific interactions with the aromatic substrate. To provide a benchmark for the role of non-specific interactions in this system, we measured the second-order rate constant for the amine-catalysed retro-aldol reaction of methodol in the presence of non-specific hydrophobic pockets such as micelles. We found that a simple micellar system, that consists of a positively-charged surfactant and a long-chain amine, can accelerate the retro-aldol reaction of methodol by 9500-fold. This effect rivals the 105-fold rate acceleration of RA-61. Similar results were obtained with BSA used as the catalyst, implying that the retro-aldol reaction of methodol can be greatly accelerated by non-specific hydrophobic pockets that contain an amino group.

Graphical abstract: The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme

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Supplementary files

Article information


Submitted
18 Sep 2013
Accepted
22 Oct 2013
First published
28 Oct 2013

Org. Biomol. Chem., 2013,11, 8419-8425
Article type
Paper

The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme

J. Schmidt, C. Ehasz, M. Epperson, K. Klas, J. Wyatt, M. Hennig and M. Forconi, Org. Biomol. Chem., 2013, 11, 8419
DOI: 10.1039/C3OB41898G

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