Symmetric versus Asymmetric Features of Homologous Homodimeric Amine Oxidases: When Water and Cavities Make the Difference

Symmetry is an intrinsic property of homo-oligomers. Amine oxidases are multidomain homodimeric enzymes that contain one catalytic site per subunit, and share a high homology degree. In this paper, we investigated, by fluorescence spectroscopy measurements, the conformational dynamics resiliency in solutions two amine oxidases, from lentil seedlings, Euphorbia characias latex, which crystallographic structure still unknown. The data demonstrate slight but significant differences exist at level local tridimensional structure, arise presence large internal cavities, characterized different hydration extents. Molecular contact network methodology were also used to further explore, silico, structural features proteins. analysis demonstrates proteins show similar long-range symmetrical connectivities, they differ their (intra-subunit) networks, appear mostly asymmetric. These have been interpreted suggest new rationale for functioning amino as obligate homodimers.