@article{oai:nagasaki-u.repo.nii.ac.jp:00002345,
 author = {Bezerra, Gustavo Arruda and Ohara-Nemoto, Yuko and Cornaciu, Irina and Fedosyuk, Sofiya and Hoffmann, Guillaume and Round, Adam and Marquez, Jose A. and Nemoto, Takayuki K. and Djinović-Carugo, Kristina},
 journal = {Scientific Reports},
 month = {Jun},
 note = {Porphyromonas gingivalis and Porphyromonas endodontalis are important bacteria related to periodontitis, the most common chronic inflammatory disease in humans worldwide. Its comorbidity with systemic diseases, such as type 2 diabetes, oral cancers and cardiovascular diseases, continues to generate considerable interest. Surprisingly, these two microorganisms do not ferment carbohydrates; rather they use proteinaceous substrates as carbon and energy sources. However, the underlying biochemical mechanisms of their energy metabolism remain unknown. Here, we show that dipeptidyl peptidase 11 (DPP11), a central metabolic enzyme in these bacteria, undergoes a conformational change upon peptide binding to distinguish substrates from end products. It binds substrates through an entropy-driven process and end products in an enthalpy-driven fashion. We show that increase in protein conformational entropy is the main-driving force for substrate binding via the unfolding of specific regions of the enzyme (“entropy reservoirs”). The relationship between our structural and thermodynamics data yields a distinct model for protein-protein interactions where protein conformational entropy modulates the binding free-energy. Further, our findings provide a framework for the structure-based design of specific DPP11 inhibitors., Scientific Reports, 7, 2848; 2017},
 title = {Bacterial protease uses distinct thermodynamic signatures for substrate recognition},
 volume = {7},
 year = {2017}
}