Abstract 1624 Determinants of oligomeric stability in a thermophilic enzyme

The oligomeric state and stabilization of an enzyme controls essential aspects of its function, including its enzymatic activity, folding, and stability. In this study, we investigated factors controlling the high oligomeric stabilization of the hexameric quaternary structure of TM0077, a thermostable esterase from Thermotoga maritima. Based on its three-dimensional structure, three distinct subregions of TM0077 were hypothesized to control the formation of its quaternary structure and to contribute to its high thermal stability.