Enzymatic MBH reaction catalyzed by an artificial enzyme designed with the introduction of an unnatural tertiary amine cofactor.
- Author:
Ya WEI
1
;
Chongwen CHEN
1
;
Yingjia TONG
1
;
Zhi ZHOU
1
Author Information
- Publication Type:Journal Article
- Keywords: Morita-Baylis-Hillman (MBH) reaction; artificial enzyme; asymmetric catalysis; biocatalysis; genetic codon expansion
- MeSH: Biocatalysis; 4-Aminopyridine/chemistry*; Enzymes/metabolism*; Coenzymes/chemistry*; Benzaldehydes/chemistry*; Protein Engineering/methods*; Click Chemistry
- From: Chinese Journal of Biotechnology 2025;41(1):376-384
- CountryChina
- Language:Chinese
- Abstract: As the chip of synthetic biology, enzymes play a vital role in the bio-manufacturing industry. The development of diverse functional enzymes can provide a rich toolbox for the development of synthetic biology. This article reports the construction of an artificial enzyme with the introduction of a non-natural cofactor. By introducing the 4-dimethylaminopyridine (DMAP) cofactor into the optimal protein skeleton via covalent bonds based on a click-chemistry strategy, we successfully constructed a novel artificial enzyme with the DMAP cofactor as the catalytic center. The artificial enzyme successfully catalyzed an unnatural asymmetric Morita-Baylis- Hillman (MBH) reaction between cycloketenone and p-nitrobenzaldehyde, with a conversion rate of 90% and enantioselectivity (e.e.) of 38%. This study not only provides an effective strategy for the design of new artificial enzymes but also establishes a theoretical basis for the development of unnatural biocatalytic MBH reactions.
