Enrico Di Cera, MD, St. Louis University

Enrico Di Cera, MD
Enrico Di Cera, MD

The Di Cera laboratory is interested in the structure and function of trypsin-like proteases, especially in the molecular determinants of substrate specificity and allosteric regulation. Their main focus is on thrombin, the key enzyme of blood coagulation and the prototypic allosteric protease. Their 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.

The Investigator's Annexe Part of The Investigator's Annexe program.



  1. Marino F, Pelc LA, Vogt A, Gandhi PS, Di Cera E. Engineering thrombin for selective specificity toward Protein C and PAR1. Journal of Biological Chemistry, 285(25):19145-19152, (2010).
  2. Dang QD, Di Cera E. A simple activity assay for thrombin and hirudin. Journal of Biological Chemistry, 285(25):19145-19152, (2010).