structure and function of D-aspartic acid-specific endopeptidase

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Paenidase is the first microorganism-derived D-aspartyl endopeptidase(Takahashi et al., J. Biochem. 2006). In this study, we revealed that the paenidase precursor was consisted of 322 amino acid residues of the mature region and 197 amino acid residues of the N-terminal extension peptide. Moreover, several mutants for the putative active site redidues of the paenidase were constructed, whereas they showed no peptidase activity. These results indicate that these residues of the paenidase are essential for the enzyme activity. We also discovered novel paenidase-inhibitors and crystallized paenidase.