Structural highlights
Publication Abstract from PubMed
We developed an artificial hydrolase based on the symmetrical Pizza6 beta-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 beta-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.
Artificial beta-propeller protein-based hydrolases.,Clarke DE, Noguchi H, Gryspeerdt JAG, De Feyter S, Voet ARD Chem Commun (Camb). 2019 Jul 23;55(60):8880-8883. doi: 10.1039/c9cc04388h. PMID:31321399[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Clarke DE, Noguchi H, Gryspeerdt JAG, De Feyter S, Voet ARD. Artificial beta-propeller protein-based hydrolases. Chem Commun (Camb). 2019 Jul 23;55(60):8880-8883. doi: 10.1039/c9cc04388h. PMID:31321399 doi:http://dx.doi.org/10.1039/c9cc04388h
