Artificial β-propeller protein-based hydrolases

DOI: 10.1039/C9CC04388H

Authors: David E. Clarke (KU Leuven) , Hiroki Noguchi (KU Leuven) , Jean-Louis A. G. Gryspeerdt (KU Leuven) , Steven De Feyter (KU Leuven) , Arnout R. D. Voet (KU Leuven)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chemical Communications , VOL 55 , PAGES 8880 - 8883

State: Published (Approved)
Published: July 2019
Diamond Proposal Number(s): 18582

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 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.

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-Macromolecular Crystallography

Added On: 31/07/2019 09:45

Discipline Tags:

Biochemistry Catalysis Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)