Jump to main content
Jump to site search

Issue 48, 2013
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 18 Sep 2013, accepted on 22 Oct 2013 and first published on 28 Oct 2013


Article type: Paper
DOI: 10.1039/C3OB41898G
Citation: Org. Biomol. Chem., 2013,11, 8419-8425
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements