E-mail a Wiley Online Library Link

Richard Obexer, Sabine Studer, Dr. Lars Giger, Dr. Daniel M. Pinkas, Prof. Markus G. Grütter, Prof. David Baker and Prof. Donald Hilvert Active Site Plasticity of a Computationally Designed Retro-Aldolase Enzyme ChemCatChem 6

Article first published online: 3 MAR 2014 | DOI: 10.1002/cctc.201300933

Thumbnail image of graphical abstract

What's that in your pocket? A computationally designed and experimentally optimized retro-aldolase enzyme utilizes amine catalysis for substrate cleavage. However, substantial differences between the original design model and experimental structure highlight the need for improved computational protocols. Generating catalysts with true enzyme-like activities will require more than simply placing a reactive lysine adjacent to a hydrophobic pocket.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field