| Function | Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides. Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. 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. 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. Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate. |
| Protein Name | Peptidyl-Glycine Alpha-Amidating MonooxygenasePam Includes - Peptidylglycine Alpha-Hydroxylating MonooxygenasePhm - Peptidyl-Alpha-Hydroxyglycine Alpha-Amidating LyasePeptidylamidoglycolate LyasePal |
| Cellular Localisation | Cytoplasmic VesicleSecretory Vesicle MembraneSingle-Pass Membrane ProteinSecretory GranulesIsoform 1: MembraneSingle-Pass Type I Membrane ProteinIsoform 2: MembraneIsoform 3: SecretedSecreted From Secretory GranulesIsoform 4: Secreted |
| Alternative Antibody Names | Anti-Peptidyl-Glycine Alpha-Amidating Monooxygenase antibodyAnti-Pam Includes - Peptidylglycine Alpha-Hydroxylating Monooxygenase antibodyAnti-Phm - Peptidyl-Alpha-Hydroxyglycine Alpha-Amidating Lyase antibodyAnti-Peptidylamidoglycolate Lyase antibodyAnti-Pal antibodyAnti-PAM antibody |
Information sourced from Uniprot.org
