Arginase: Structure, Function, and Therapeutic Targeting

Luigi F. Di Costanzo is a structural chemist and biochemist specializing in structural biology, enzymology, and protein science, with a focus on metalloenzymes and structure-based approaches to enzyme function and inhibition. He earned his Ph.D. in Chemistry from the Università degli Studi di Trieste (Italy) and completed postdoctoral training at the University of Pennsylvania, where he contributed to foundational studies on enzyme structure and inhibitor design. His research centers on the three-dimensional structure and mechanism of enzymes, with extensive experience in macromolecular crystallography, including structure determination, refinement, and analysis of protein–ligand complexes. His work integrates structural, biochemical, and biophysical approaches to understand enzyme function and guide therapeutic targeting. In addition to his research, he served for over a decade as a biocurator with the Worldwide Protein Data Bank (wwPDB) at the RCSB PDB (Rutgers University), contributing to the validation and annotation of more than 7,500 macromolecular structures. This work supported the integrity and reproducibility of structural biology data used by the global scientific community, including structural datasets that have contributed to the development of machine learning approaches to protein structure prediction, such as AlphaFold. His broader expertise includes multiscale structural characterization through complementary imaging and analytical techniques, including X-ray micro–computed tomography (μCT), linking atomic-level structure to complex biological systems, as well as contributions to community data resources, including the Protein Design Archive. As editor of the Methods in Enzymology volume “Arginase: Structure, Function, and Therapeutic Targeting, he brings together structural, metabolic, and translational perspectives to advance the field.