The function of PAM (peptidylglycine alpha-amidating monooxygenase, ENSG00000145730) is as follows. Bifunctional enzyme that catalyzes amidation of the C- terminus of proteins (PubMed:12699694, PubMed:2357221). Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity (PubMed:1575450). C- terminal amidation also takes place in response to protein fragmentation triggered by oxidative stress, promoting degradation of amidated protein fragments by the proteasome (PubMed:2207077). Alpha- amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme (PubMed:12699694). The first step, catalyzed by peptidyl alpha- hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:12699694). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc- dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:12699694). Similarly, catalyzes the two- step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity). {ECO:0000250|UniProtKB:P14925, ECO:0000269|PubMed:12699694, ECO:0000269|PubMed:2357221, ECO:0000303|PubMed:1575450, ECO:0000303|PubMed:2207077}.