Editorial [Hot topic: Latest Development on Zinc Enzymes (Executive Editor: Georgios A. Spyroulias)]

Zinc (Zn) metal ion along with other transition metals like copper and iron are of vital significance in living organisms with zinc being the second most abundant transition metal ion in living organism following iron. Zn(II) exhibits remarkable stability in redox processes due to its d10 electronic configuration and is known to be indispensable to growth and development, to metabolic pathways as well as to transmission of the genetic message. The coordination properties of the zinc that allows the metal to bind within a broad range of tetrahedral sites in proteins can discriminate the role of zinc in four classes, such as catalytic, cocatalytic, structural and protein interface. Zinc metal sites are encountered in a wide variety of enzymes implicated in synthesis of nucleic acid and proteins, catalysis, protein/peptide degradation, signaling etc. Recent studies propose that zinc proteins may comprise the 10% of the human proteome. In this issue of Current Pharmaceutical Design journal a variety of zinc enzymes are discussed and the latest achievements in the study of their structural and functional properties are highlighted along with the recent developments in the design and biological properties of new zinc chelators, which might act as modulators of enzymes’ function, with potential interest in pharmacology and medicine. I. Bertini and co-workers [1] at the Center of Magnetic Resonance and the University of Florence (Italy) provide a report on the recent advances in Matrix Metalloproteases genetics and function, highlighting the variability of the structural features among the family of these enzymes along with their intra- or inter-domain dynamics that are also taken into account in latest attempts for design and biological evaluation of new inhibitors.