Download MendeleyArtificial beta-propeller protein-based hydrolases.
Clarke, D.E., Noguchi, H., Gryspeerdt, J.A.G., De Feyter, S., Voet, A.R.D.(2019) Chem Commun (Camb) 55: 8880-8883
- PubMed: 31321399
- DOI: https://doi.org/10.1039/c9cc04388h
- Primary Citation of Related Structures:
6REG, 6REH, 6REJ, 6REK, 6REN - PubMed 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.
Organizational Affiliation:
Division of Molecular Imaging and Photonics, Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001, Leuven, Belgium.
