Enrico Di Cera, M.D.
Alice A. Doisy Professor and Chairman
Structure and function of trypsin-like proteases, such as thrombin, and the molecular determinants of substrate specificity and allosteric regulation.
Office: DRC, Room 533
Voice: (314) 977-9201
M.D., 1985, Catholic University School of Medicine, Rome, Italy.
We are interested in the structure and function of trypsin-like proteases, especially in the molecular determinants of substrate specificity and allosteric regulation. Our main focus is on thrombin, the key enzyme of blood coagulation and the prototypic allosteric protease. Our experimental approaches encompass enzyme kinetics (steady state and pre-steady state), thermodynamics (calorimetry), site-directed mutagenesis, protein engineering and X-ray structural biology. Our theoretical approaches involve linkage, allostery and site-specific thermodynamics.
- Autoactivation of thrombin precursors.
Pozzi N, Chen Z, et al. J Biol Chem. (2013) 288(16):11601-10.
- Conformational selection or induced fit? A critical appraisal of the kinetic mechanism.
Vogt AD and Di Cera E. Biochemistry. (2012) 51(30):5894-902.
- Conformational selection in trypsin-like proteases.
Pozzi N, Vogt AD, et al. Curr Opin Struct Biol. (2012) 22(4):421-31.
- Exposure of R169 controls protein C activation and auto activation.
Pozzi N, Barranco-Medina S, et al. Blood. (2012) 120(3):664-70.
- Thrombomodulin is required for the antithrombotic activity of thrombin mutant W215A/E217A in a mouse model of arterial thrombosis.
Vicente CP, et al. Thromb Res. (2012) 130(4):646-8.