Title
Towards the de novo design of metallohydrolases
Conference Dates
September 15-19, 2019
Abstract
De novo design of proteins has enabled the exploration of vast regions of sequence space previously inaccessible by nature.[1] These proteins are computationally designed based on physical principles of protein structure and folding, and are tailored according to a specific function or property. Great advances have been made in the design of novel highly stable protein folds capable of hosting enzyme active sites.[2] That has in turn allowed us to undertake larger scale efforts of installing various enzymatic activity into these scaffolds. As a proof of principle we have undertaken efforts towards designing hydrolase (esterase and phosphatase) activity into the NTF2[2b] and the TIM-barrel[3] folds through the introduction of metal binding sites.
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Recommended Citation
Indrek Kalvet and David Baker, "Towards the de novo design of metallohydrolases" 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/64