Cupin Variants as Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes

31 December 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantio-selective Michael addition reaction of nitroalkanes to an α,β-unsaturated ketone. Moreover, in silico substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.

Keywords

artificial metalloenzymes
Cupin Superfamily
Macromolecular Ligands
Stereodivergent Synthesis
protein library

Supplementary materials

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Description
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Title
SI 191231 NF
Description
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