Artificial β-propeller protein-based hydrolases. Issue 60 (19th July 2019)

• Record Type: Journal Article
• Authors: Clarke, David E.; Noguchi, Hiroki; Gryspeerdt, Jean-Louis A. G.; De Feyter, Steven; Voet, Arnout R. D.
• Is Part Of: Chemical communications. Volume 55:Issue 60(2019)
• Page Start: 8880
• Page End: 8883
• Publication Date: 2019-07-19
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c9cc04388h
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : We investigated symmetrical β-propeller protein scaffolds as artificial hydrolases and discovered their catalytic mechanism to be centred around a threonine–histidine dyad. Abstract : 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 k cat 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.