Enzymology. Coordinator: Hochkoeppler

The research activity of the enzymology group aims at the understanding of enzymes, their functions, and their applications. The main focus concerns how enzymes catalyze biochemical reactions at the molecular level, including the identification of active sites, allosteric sites and substrates. Our research is also dedicated to investigate how enzymes are regulated within biological systems, including the effects of inhibitors, activators, and environmental conditions.

Areas: Industrial, plant and environmental biotechnologies

Research themes

Our research group is mainly involved in the following projects: 1) study of the assembly of tetrameric human lactate dehydrogenase LDH-5 using the monomeric protein, LDH-A; 2) characterization of linear and cyclic peptides capable of interfering with the assembly of the tetrameric enzyme; 3) effect of trehalose on the activity of rabbit muscle lactate dehydrogenase; 4) expression in Escherichia coli and purification of the recombinant D-lactate human dehydrogenase.

Lab Members

Alejandro Hochkoeppler, Associate Professor

Alessandra Stefan, Assistant Professor

Antonio Gonzalez Vara y Rodriguez, Assistant Professor

Internship projects

1 intership project: analysis of the stabilization of the rabbit muscle lactate dehydrogenase (LDH) induced by trehalose and study of the conformational rearrangements induced by the disaccharide.

Main publications

Stefan, A., Gentilucci, L., Ruffolo, F., Rossi, V., Sordi, S., He, T., di Stefano, G., Santino, F., Brigotti, M., Scotti, C., Iamele, L., de Jonge, H. and Hochkoeppler A. (2024). “Peptides inhibiting the assembly of monomeric human l-lactate dehydrogenase into catalytically active homotetramer decrease the synthesis of lactate in cultured cells.” Protein Science 33(10): e5161.Doi: 1002/pro.5161
Stefan, A., Mucchi, A. and Hochkoeppler A. (2024). “The catalytic action of human D-lactate dehydrogenase is severely inhibited by oxalate and is impaired by mutations triggering D-lactate acidosis.” Archives of Biochemistry and Bioplysics754: 109932. Doi: 1016/j.abb.2024.109932
Simongini, M., Puglisi, A., Genovesi, F. and Hochkoeppler A. (2023). “Trehalose counteracts the dissociation of tetrameric rabbit lactate dehydrogenase induced by acidic pH conditions.” Archives of Biochemistry and Bioplysics 740: 109584. Doi: 1016/j.abb.2023.109584
Iacovino, L.G., Rocci, M., di Stefan, G., Rossi, V., Binda, C., Brigotti, M., Tomaselli, F., Pasti, AP., Dal Piaz, F., Cerini, S. and Hochkoeppler A. (2022). “Allosteric transitions of rabbit skeletal muscle lactate dehydrogenase induced by pH-dependent dissociation of the tetrameric enzyme.” Biochimie 199: 23-35. Doi: 1016/j.biochi.2022.03.008
Pasti, A.P., Rossi, V., di Stefano, G., Brigotti, M. and Hochkoeppler A. (2022). “Human lactate dehydrogenase A undergoes allosteric transitions under pH conditions inducing the dissociation of the tetrameric enzyme.” Biosci Rep 42(1):20212654. Doi: 1042/BSR20212654

Contacts

Alejandro Hochkoeppler

Associate Professor

Department of Pharmacy and Biotechnologies

UE5 – Plesso Navile – primo piano

Via Piero Gobetti 87, Bologna.

a.hochkoeppler@unibo.it

Tel: +390512093671