Computational protein design methods were used to predict five variants of monofunctional Escherichia coli chorismate mutase expected to maintain catalytic activity. The variants were tested experimentally and three active site mutants exhibited catalytic activity similar to or greater than the wild-type enzyme. One mutant, Ala32Ser, showed increased catalytic efficiency.

Download full-text PDF

Source
http://dx.doi.org/10.1093/protein/gzi015DOI Listing

Publication Analysis

Top Keywords

catalytic activity
12
escherichia coli
8
coli chorismate
8
chorismate mutase
8
computationally designed
4
designed variants
4
variants escherichia
4
mutase altered
4
catalytic
4
altered catalytic
4

Similar Publications

This study reports on the development of a highly sensitive non-enzymatic electrochemical sensor based on a two-dimensional TiCT/MWCNT-OH nanocomposite for the detection of paraoxon-based pesticide. The synergistic effect between the TiCT nanosheet and the functionalized multi-walled carbon nanotubes enhanced the sensor's conductivity and catalytic activity. The nanocomposite demonstrates superior electrochemical and electroanalytical performance compared to the pristine TiCT and MWCNT-OH in detecting paraoxon-ethyl in fruit samples (green and red grapes), with a linear response range from 0.

View Article and Find Full Text PDF

Affinity descriptor of metal catalysts: concept, measurement and application of oxygen affinity in the catalytic transformation of oxygenates.

Chem Soc Rev

January 2025

National-local Joint Engineering Research Center of Biomass Refining and High-quality Utilization, Changzhou University, Changzhou 213164, China.

Multiple oxygenate groups in biomass-based feedstocks are open to multiple catalytic pathways and products, typically resulting in low selectivity for the desired products. In this context, strategies for rational catalyst design are critical to obtain high selectivity for the desired products in biomass upgrading. The Sabatier principle provides a conceptual framework for designing optimal catalysts by following the volcanic relationship between catalyst activity for a reaction and the binding strength of a substrate on a catalyst.

View Article and Find Full Text PDF

Mass transfer governs the overall catalytic performance of heterogeneous catalysts considerably; however, this fundamental research has often been ignored. Here, macroporous SiO-supported Pt nanoparticle (Pt/SiO-M) and mesoporous SiO-supported Pt nanoparticle (Pt/SiO-m) catalysts were specifically fabricated by a facile thermal reduction step to engineer the resultant Pt nanoparticles showing similar physiochemical properties while possessing completely different porous microstructures exclusively originating from SiO supports. On this basis, a platform to explore the crucial mass transfer difference affecting catalytic activity is then established by systematically practicing industry-important benzene oxidation measurements.

View Article and Find Full Text PDF

This research highlights a sustainable approach for the design and synthesis of a magnetic nickel ferrite (NiFeO) catalyst reutilizing industrial waste, specifically iron ore tailing and Raney nickel catalyst processing waste, by simple co-precipitation method. Transforming waste materials into high-performance catalysts, this study aligns with the principles of a circular economy, addressing both environmental waste and pollution. Structural characterization by X-ray diffraction (XRD) and microscopic (FESEM and TEM) revealed the formation of well crystalline nano ferrite with NiFeO nanoparticles with cubic spinel structure.

View Article and Find Full Text PDF

Self-sufficient biocatalytic cascade for the continuous synthesis of danshensu in flow.

Appl Microbiol Biotechnol

January 2025

Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland.

A new strategy has been developed to successfully produce the active component danshensu ex vivo. For this purpose, phenylalanine dehydrogenase from Bacillus sphaericus was combined with the novel hydroxyphenylpyruvate reductase from Mentha x piperita, thereby providing an in situ cofactor regeneration throughout the conversion process. The purified enzymes were co-immobilized and subsequently employed in batch biotransformation, resulting in 60% conversion of 10 mM L-dopa within 24 h, with a catalytic amount of NAD as cofactor.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!