Work

Carbonic anhydrase mimics with rationally designed active sites for fine-tuned catalytic activity and selectivity in ester hydrolysis

Year: 2023

Type: article

Abstract: of 6.3-6.4 for zinc-bound water is lower than the 6.8-7.3 value for natural enzymes, which allows the catalyst to hydrolyze nonactivated alkyl esters under neutral conditions-a long sought-after goal for artificial esterases. The size and shape of the active site can be rationally tuned through a template used in molecular imprinting. Subtle structural changes in the template, including shifting an ethyl group by one C-N bond and removal of a methylene group, correlate directly with catalytic activity. A catalyst can be made to be highly specific or have broad substrate specificity through modular synthesis of templates.

Source: Catalysis Science & Technology

DOI: 10.1039/d3cy00704a

Authors: Foroogh Bahrami, Yan Zhao

Institution: Iowa State University

Language: English

Topic: Enzyme function and inhibition

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Funder: National Institute of General Medical Sciences

Award: Artificial Glycosidase with Controlled Selectivity