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Evolution-based model for designing chorismate mutase enzymes

July 28th, 2020

The rational design of enzymes is an important goal for both fundamental and practical reasons. Here, we describe a process to learn the constraints for specifying proteins purely from evolutionary sequence data, design and build libraries of synthetic genes, and test them for activity in vivo using a quantitative complementation assay. For chorismate mutase, a key enzyme in the biosynthesis of aromatic amino acids, we demonstrate the design of natural-like catalytic function with substantial sequence diversity. Further optimization focuses the generative model towards function in a specific genomic context. The data show that sequence-based statistical models suffice to specify proteins and provide access to an enormous space of functional sequences. This result provides a foundation for a general process for evolution-based design of artificial proteins.

More information:
science.sciencemag.org/content/369/6502/440
DOI: 10.1126/science.aba3304
Rémi Monasson - Simona Cocco
Laboratoire de Physique de L’Ecole normale supérieure (LPENS, ENS Paris/CNRS/Sorbonne Université/Université de Paris)

Provided by The Physics Laboratory of the Ecole Normale Supérieure

Citation: Evolution-based model for designing chorismate mutase enzymes (2020, July 28) retrieved 13 November 2024 from https://sciencex.com/wire-news/357378151/evolution-based-model-for-designing-chorismate-mutase-enzymes.html

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