DPEP2 belongs to the membrane-bound dipeptidase (EC 3.4.13.19) family. These enzymes hydrolyze a variety of dipeptides, including leukotriene D4, the beta-lactam ring of some antibiotics, and cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation.The deduced 578-amino acid mouse protein contains several residues conserved among MBDs, including 6 cysteines, 3 histidines, and a glutamic acid that is important for catalytic activity. Mouse and human MBD2 share 80% amino acid identity. Spleen, liver, and skeletal muscle expressed low Mbd2 levels, and no expression was detected in kidney and brain. Phospholipase treatment released Mbd2 from transfected COS-7 cell membranes, indicating that Mbd2 is anchored to the membrane through glycosylphosphatidylinositol modification.