Post-transcriptional association of proteins to study spatial organisation within multi-enzyme complexes
Résumé
To catalyse chemical reactions, nature has evolved enzymatic cascades. These multistep reactions in living cells are often performed by multi-enzyme complexes to maintain high local concentrations of intermediates to enhance reaction rates, called substrate channelling. Based on the fact that natural proteins or nucleic acid-protein interactions can be used as scaffolds for the construction of functional multi-enzyme complexes, artificial scaffolds have been developed for the construction of multi-enzyme complexes which carry out multi-step enzymatic catalysis processes1. However, none of them have systematically investigated the spatial organisation of the enzymes and its effect on the product(s) released.
We are investigating this question using the Molecular Welding Tool2 consisting of two small proteins, Jo and In, which spontaneously form an intramolecular isopeptide bond and, incidentally, provide an original means of orienting enzymes3,4.
Fichier principal
Poster-Montanier-enzyme engineering-2023.09.25.pdf (1.46 Mo)
Télécharger le fichier
Origine | Fichiers produits par l'(les) auteur(s) |
---|