PAM 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 monoxygenase (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. In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family. 6 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC; EC; Lyase; Membrane protein, integral; Oxidoreductase; Vesicle
Chromosomal Location of mouse Ortholog: 1 D|1 47.76 cM
Cellular Component:  cell surface; cytoplasmic vesicle; cytosol; extracellular region; extracellular space; membrane; neuronal cell body; perikaryon; perinuclear region of cytoplasm; plasma membrane; secretory granule; trans-Golgi network
Molecular Function:  calcium ion binding; catalytic activity; copper ion binding; identical protein binding; L-ascorbic acid binding; lyase activity; metal ion binding; monooxygenase activity; oxidoreductase activity; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; peptidylamidoglycolate lyase activity; peptidylglycine monooxygenase activity; protein kinase binding; zinc ion binding
Biological Process:  fatty acid primary amide biosynthetic process; lipid metabolic process; long-chain fatty acid metabolic process; metabolic process; peptide amidation; peptide metabolic process; protein amidation; regulation of actin cytoskeleton organization; regulation of transcription by RNA polymerase II; response to pH; response to xenobiotic stimulus; response to zinc ion; toxin metabolic process
Reference #:  P97467 (UniProtKB)
Alt. Names/Synonyms: AMD; PAL; PAM; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidyl-glycine alpha-amidating monooxygenase; PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE PRECURSOR (PAM); Peptidylamidoglycolate lyase; peptidylglycine alpha-amidating monooxygenase; Peptidylglycine alpha-hydroxylating monooxygenase; PHM
Gene Symbols: Pam
Molecular weight: 108,963 Da
Basal Isoelectric point: 6.1  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein