Protein scaffolds: A tool for multi-enzyme assembly

Abstract

Highlights Protein scaffold acts as a backbone with several interacting domains and ligands for the integration of specific enzymes. Different protein-enzyme ligation strategies are used for the co-localization of enzymes. Scaffolds permit control over spatial organization, enzyme stoichiometry, and proximity. Improvement in pathway flux and product yield can be achieved with scaffold-based multi-enzyme complex. Various analytical tools are utilized to study the multi-enzyme assembly process.

The optimal docking strength for reversibly tethered kinases

“…33 These interactions allow connections to different upstream and downstream partners ultimately making these systems highly evolvable and adaptable 34 . Modularity has been also exploited in biotechnology, bioengineering and pharmacology 35,36,37 to successfully rewire signaling processes or modify enzymatic activities. This emergent class of engineered multi-domain proteins relies on easy transfer and exchange 34 of modules, such that design boils down to selecting the right connectors.…”

Peptide-Inspired One-Step Synthesis of Surface-Functionalized Fe3O4 Magnetic Nanoparticles for Oriented Enzyme Immobilization and Biocatalytic Applications

“…Covalent bonds are usually more efficient in recycling, and sometimes, they can achieve oriented immobilization. , As we know, most oriented immobilization is needed to coat carriers with organic reagents or other materials with functional groups; , for example, the formation of reversible Au–S bonds for trypsin immobilization, which preserved the native conformation of the trypsin well, − but this method is not applicable to MNPs. In addition, coimmobilization was another effective way to maximize the recovery rate of activity and maintain the structure of the enzymes . However, it also has some drawbacks: it is only suitable for small substrates which can easily diffuse into the active sites of the immobilized enzyme.…”

“…In addition, coimmobilization was another effective way to maximize the recovery rate of activity and maintain the structure of the enzymes. 14 However, it also has some drawbacks: it is only suitable for small substrates which can easily diffuse into the active sites of the immobilized enzyme. Thus, it is urgent to select an appropriate immobilization method according to the characteristics of the target enzymes.…”

Programming an Orthogonal Self-Assembling Protein Cascade Based on Reactive Peptide–Protein Pairs for In Vitro Enzymatic Trehalose Production

“…The widespread application of protein nanostructures in the construction of multienzyme systems with controllable spatial arrangement and precise location proves their potential as universal scaffolds. − Nature has developed a series of strategies to create self-assembling protein nanostructures with highly specialized biological functions. , The ethanolamine utilization (Eut) bacterial microdomain (BMC) of Salmonella enterica is a special protein nanostructure, which can prevent the volatile intermediate acetaldehyde from entering the cytoplasm to reduce its toxicity . The shell plane protein (EutM) of the microcompartment (Eut-BMC) can self-assemble into hexamers, and these basic building blocks pack tightly side by side into a molecular layer or sheet (Figure a). − EutM can self-assemble in the form of large protein filaments in vivo and crystal arrays in vitro .…”