Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme

Daniel W. Watkins, Jonathan M. X. Jenkins, Katie J. Grayson, Nicola Wood, Jack W. Steventon, Kristian K. Le Vay, Matthew I. Goodwin, Anna S. Mullen, Henry J. Bailey, Matthew P. Crump, Fraser MacMillan, Adrian J. Mulholland, Gus Cameron, Richard B. Sessions, Stephen Mann and J. L. Ross Anderson ()
Additional contact information
Daniel W. Watkins: University of Bristol, University Walk
Jonathan M. X. Jenkins: University of Bristol, University Walk
Katie J. Grayson: University of Bristol, University Walk
Nicola Wood: University of Bristol, University Walk
Jack W. Steventon: University of Bristol, University Walk
Kristian K. Le Vay: University of Bristol, University Walk
Matthew I. Goodwin: University of Bristol
Anna S. Mullen: University of East Anglia
Henry J. Bailey: University of Bristol, University Walk
Matthew P. Crump: University of Bristol
Fraser MacMillan: University of East Anglia
Adrian J. Mulholland: University of Bristol
Gus Cameron: University of Bristol, University Walk
Richard B. Sessions: University of Bristol, University Walk
Stephen Mann: University of Bristol
J. L. Ross Anderson: University of Bristol, University Walk

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract Although catalytic mechanisms in natural enzymes are well understood, achieving the diverse palette of reaction chemistries in re-engineered native proteins has proved challenging. Wholesale modification of natural enzymes is potentially compromised by their intrinsic complexity, which often obscures the underlying principles governing biocatalytic efficiency. The maquette approach can circumvent this complexity by combining a robust de novo designed chassis with a design process that avoids atomistic mimicry of natural proteins. Here, we apply this method to the construction of a highly efficient, promiscuous, and thermostable artificial enzyme that catalyzes a diverse array of substrate oxidations coupled to the reduction of H2O2. The maquette exhibits kinetics that match and even surpass those of certain natural peroxidases, retains its activity at elevated temperature and in the presence of organic solvents, and provides a simple platform for interrogating catalytic intermediates common to natural heme-containing enzymes.

Date: 2017
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DOI: 10.1038/s41467-017-00541-4

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