Active Site Plasticity of a Computationally Designed Retro-Aldolase Enzyme (pages 1043–1050)
Richard Obexer, Sabine Studer, Dr. Lars Giger, Dr. Daniel M. Pinkas, Prof. Markus G. Grütter, Prof. David Baker and Prof. Donald Hilvert
Version of Record online: 3 MAR 2014 | DOI: 10.1002/cctc.201300933
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.