Design strategy for creating catalytically active metal binding proteins
September 15-19, 2019
Metalloenzymes catalyze a wide variety of reactions in nature by taking advantage of the versatility and reactivity of transition metals. Despite the diversity of reactions catalyzed by natural proteins, there is still a demand for designer enzymes. In many cases, all that is needed is routine re-engineering of the native enzymes to perform efficiently under the demanded application conditions. In other cases, the reaction or reaction condition desired differs so much from natural conditions that mere redesign of natural proteins is not practical. De novo enzymes, which are generated entirely from first principles rather than modified from natural proteins, are ideal for these situations. These de novo enzymes would allow us to generate enzymes that can survive at much higher temperatures, work in many different solvents and solutions, or perform completely novel functions.
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Stacey Gerben, Ralph Cacho, and David Baker, "Design strategy for creating catalytically active metal binding proteins" in "Enzyme Engineering XXV", Huimin Zhao, University of Illinois at Urbana-Champaign, USA John Wong, Pfizer, USA Eds, ECI Symposium Series, (2019). https://dc.engconfintl.org/enzyme_xxv/26