A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase

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ID: 261233
2020
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Abstract
While the bottom-up design of enzymes appears to be an intractably complex problem, a minimal approach that combines elementary, de novo-designed proteins with intrinsically reactive cofactors offers a simple means to rapidly access sophisticated catalytic mechanisms. Not only is this method proven in the reproduction of powerful oxidative chemistry of the natural peroxidase enzymes, but we show here that it extends to the efficient, abiological—and often asymmetric—formation of strained cyclopropane rings, nitrogen–carbon and carbon–carbon bonds, and the ring expansion of a simple cyclic molecule to form a precursor for NAD+, a fundamentally important biological cofactor. That the enzyme also functions in vivo paves the way for its incorporation into engineered biosynthetic pathways within living organisms.
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stenner2020proceedingsa Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Richard Stenner;Jack W. Steventon;Annela Seddon;J. L. Ross Anderson;Richard Stenner;Jack W. Steventon;Annela Seddon;J. L. Ross Anderson;
Journal proceedings of the national academy of sciences
Year 2020
DOI
10.1073/pnas.1915054117
URL
https://dx.doi.org/10.1073/pnas.1915054117
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