Puromycin is a reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). Dipeptides are produced from polypeptides by the action of the hydrolase enzyme dipeptidyl peptidase. Other members of this family include the mitochondrial processing peptidase and presequence protease. These enzymes include peptidase, sucrase, maltase, lactase and intestinal lipase. The eukaryotic signal peptidase is an integral membrane protein complex. Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. The saccharopepsin inhibitor I34 is highly specific for the aspartic peptidase saccharopepsin. Members of this family are the peptidase inhibitor madanin proteins. This enzyme belongs to the peptidase family C60. This enzyme is part of the papain-like peptidase C1 family. Sitagliptin works to competitively inhibit the enzyme dipeptidyl peptidase 4 (DPP-4). Each family, clan, peptidase, and inhibitor has a unique identifier. Trypsin, a type of peptidase, is a digestive enzyme active in the duodenum and elsewhere. The conserved domain contains a DNA binding structure and a peptidase fold. The signal peptide is typically removed at the destination by a signal peptidase.