摘要
The aminoacylhistidine dipeptidase (PepD) protein encoded by Vibrio alginolyticus pepD was successfully overexpressed and characterized and the putative active-site residues responsible for metal binding and catalysis were identified. The purified enzyme contained two zinc ions per monomer. The recombinant dipeptidase enzyme, which was identified as a homodimer in solution, exhibited broad substrate specificity for Xaa-His dipeptides, with highest activity towards the His-His dipeptide. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Preliminary crystallographic analysis showed that the crystal belonged to space group P6 1 or P6 5 , with unit-cell parameters a = b = 80.42, c = 303.11 Å. The crystal contained two molecules per asymmetric unit and the predicted solvent content was 53.4%. © 2009 International Union of Crystallography All rights reserved.