Peptidylglycine alpha-Amidating Monooxygenase/PAM: Products
PAM (Peptidyl-Gly alpha-amidating monooxygenase) is a dual-function, 95-110 kDa 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 953 amino acid (aa) type I transmembrane glycoprotein. It contains an 833 aa extracellular domain (ECD) (aa 31-863) and an 86 aa cytoplasmic tail. The ECD shows one PHM/monooxygenase region (aa 40-347) and a PAL/lyase domain (aa 495-817). Both regions are enzymatically active. Alternative splicing may generate a soluble form (aa 31-828), and remove aa 388-494 that link the two embedded enzyme segments. Over aa 21-817, human PAM is 91% aa identical to mouse PAM.
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