PAM (Peptidyl-Gly alpha-amidating monooxygenase) is a dual-function, 95-110kD protein that belongs to both the lyase and monooxygenase enzyme families. It is expressed in a variety of endocrine and exocrine glands and catalyzes the conversion of C-terminal Gly into amidated residues. Human ProPAM is a 953aa type I transmembrane glycoprotein. It contains an 833 aa extracellular domain (ECD) (aa31-863) and an 86 aa cytoplasmic tail. The ECD shows one PHM/monooxygenase region (aa40-347) and a PAL/lyase domain (aa495-817). Both regions are enzymatically active. Alternative splicing may generate a soluble form (aa31-828), and remove aa388-494 that link the two embedded enzyme segments. Over aa 1-817, human PAM is 91% aa identical to mouse PAM.