Towards the de novo design of metallohydrolases
September 15-19, 2019
De novo design of proteins has enabled the exploration of vast regions of sequence space previously inaccessible by nature. 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. 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 folds through the introduction of metal binding sites.
Please click Additional Files below to see the full abstract.
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