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Issue 60, 2019

Artificial β-propeller protein-based hydrolases

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We developed an artificial hydrolase based on the symmetrical Pizza6 β-propeller protein for the metal-free hydrolysis of 4-nitrophenyl acetate and butyrate. Through site-specific mutagenesis and crystallisation studies, the catalytic mechanism was investigated and found to be dependent on a threonine–histidine dyad. The mutant with additional histidine residues generated the highest kcat values, forming a His–His–Thr triad and matched previously reported metalloenzymes. The highly symmetrical β-propeller artificial enzymes and their protein–metal complexes have potential to be utilised in bioinorganic and supramolecular chemistry, as well as being developed further into 2D/3D catalytic materials.

Graphical abstract: Artificial β-propeller protein-based hydrolases

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Article information

07 Jun 2019
03 Jul 2019
First published
04 Jul 2019

Chem. Commun., 2019,55, 8880-8883
Article type

Artificial β-propeller protein-based hydrolases

D. E. Clarke, H. Noguchi, J. A. G. Gryspeerdt, S. De Feyter and A. R. D. Voet, Chem. Commun., 2019, 55, 8880 DOI: 10.1039/C9CC04388H

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