Jump to main content
Jump to site search
SCHEDULED MAINTENANCE Close the message box

Maintenance work is planned for Monday 16 August 2021 from 07:00 to 23:59 (BST).

Website performance may be temporarily affected and you may not be able to access some PDFs or images. If this does happen, refreshing your web browser should resolve the issue. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 60, 2019

Artificial β-propeller protein-based hydrolases

Author affiliations

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.

Graphical abstract: Artificial β-propeller protein-based hydrolases

Supplementary files

Article information


Submitted
07 Jun 2019
Accepted
03 Jul 2019
First published
04 Jul 2019

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

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.


Social activity

Search articles by author

Spotlight

Advertisements