Modregger J

References (3)

Title : Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor - Fernandez-Lopez_2023_Chem.Commun.(Camb)__
Author(s) : Fernandez-Lopez L , Cea-Rama I , Alvarez-Malmagro J , Ressmann AK , Gonzalez-Alfonso JL , Coscolin C , Shahgaldian P , Plou FJ , Modregger J , Pita M , Sanz-Aparicio J , Ferrer M
Ref : Chem Commun (Camb) , : , 2023
Abstract : Metal complexes introduced into protein scaffolds can generate versatile biomimetic catalysts endowed with a variety of catalytic properties. Here, we synthesized and covalently bound a bipyridinyl derivative to the active centre of an esterase to generate a biomimetic catalyst that shows catecholase activity and enantioselective catalytic oxidation of (+)-catechin.
ESTHER : Fernandez-Lopez_2023_Chem.Commun.(Camb)__
PubMedSearch : Fernandez-Lopez_2023_Chem.Commun.(Camb)__
PubMedID: 37376994
Gene_locus related to this paper: 9zzzz-a0a2k8jn75

Title : Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis - Alonso_2020_Nat.Catal_3_319
Author(s) : Alonso S , Santiago G , Cea-Rama I , Fernandez-Lopez L , Coscolin C , Modregger J , Ressmann A , Martinez-Martinez M , Marrero H , Bargiela R , Pita M , Gonzalez-Alfonso JL , Briand M , Rojo D , Barbas C , Plou FJ , Golyshin PN , Shahgaldian P , Sanz-Aparicio J , Guallar V , Ferrer M
Ref : Nature Catalysis , 3 :319 , 2019
Abstract : Enzyme engineering has allowed not only the de novo creation of active sites catalysing known biological reactions with rates close to diffusion limits, but also the generation of abiological sites performing new-to-nature reactions. However, the catalytic advantages of engineering multiple active sites into a single protein scaffold are yet to be established. Here, we report on pro-teins with two active sites of biological and/or abiological origin, for improved natural and non-natural catalysis. The approach increased the catalytic properties, such as enzyme efficiency, substrate scope, stereoselectivity and optimal temperature window, of an esterase containing two biological sites. Then, one of the active sites was metamorphosed into a metal-complex chemocatalytic site for oxidation and Friedel-Crafts alkylation reactions, facilitating synergistic chemo- and biocatalysis in a single protein. The transformations of 1-naphthyl acetate into 1,4-naphthoquinone (conversion approx. 100%) and vinyl crotonate and benzene into 3-phenylbutyric acid (>=83%; e.e. >99.9%) were achieved in one pot with this artificial multifunc-tional metalloenzyme.
ESTHER : Alonso_2020_Nat.Catal_3_319
PubMedSearch : Alonso_2020_Nat.Catal_3_319
PubMedID:
Gene_locus related to this paper: 9bact-LAE6

Title : Phosphorylation of a synaptic vesicle-associated protein by an inositol hexakisphosphate-regulated protein kinase - Hilton_2001_J.Biol.Chem_276_16341
Author(s) : Hilton JM , Plomann M , Ritter B , Modregger J , Freeman HN , Falck JR , Krishna UM , Tobin AB
Ref : Journal of Biological Chemistry , 276 :16341 , 2001
Abstract : Despite the fact that inositol hexakisphosphate (InsP(6)) is the most abundant inositol metabolite in cells, its cellular function has remained an enigma. In the present study, we present the first evidence of a protein kinase identified in rat cerebral cortex/hippocampus that is activated by InsP(6). The substrate for the InsP(6)-regulated protein kinase was found to be the synaptic vesicle-associated protein, pacsin/syndapin I. This brain-specific protein, which is highly enriched at nerve terminals, is proposed to act as a molecular link coupling components of the synaptic vesicle endocytic machinery to the cytoskeleton. We show here that the association between pacsin/syndapin I and dynamin I can be increased by InsP(6)-dependent phosphorylation of pacsin/syndapin I. These data provide a model by which InsP(6)-dependent phosphorylation regulates synaptic vesicle recycling by increasing the interaction between endocytic proteins at the synapse.
ESTHER : Hilton_2001_J.Biol.Chem_276_16341
PubMedSearch : Hilton_2001_J.Biol.Chem_276_16341
PubMedID: 11278843