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 1.14.17.3; EC 4.3.2.5; Lyase; Membrane protein, integral; Oxidoreductase; Vesicle
Chromosomal Location of rat Ortholog: 9q37
Cellular Component:  cell surface; extracellular region; extracellular space; integral component of membrane; neuron projection; neuronal cell body; perikaryon; perinuclear region of cytoplasm; plasma membrane; secretory granule; secretory granule membrane; trans-Golgi network; transport vesicle membrane
Molecular Function:  calcium ion binding; copper ion binding; L-ascorbic acid binding; peptidylamidoglycolate lyase activity; peptidylglycine monooxygenase activity; protein binding; protein kinase binding; zinc ion binding
Biological Process:  central nervous system development; heart development; lactation; limb development; long-chain fatty acid metabolic process; maternal process involved in female pregnancy; odontogenesis; ovulation cycle process; oxidation-reduction process; peptide amidation; peptide metabolic process; protein amidation; protein homooligomerization; protein metabolic process; regulation of actin cytoskeleton organization; regulation of protein secretion; regulation of transcription by RNA polymerase II; response to copper ion; response to drug; response to estradiol; response to glucocorticoid; response to hypoxia; response to pH; toxin metabolic process
Reference #:  P14925 (UniProtKB)
Alt. Names/Synonyms: AMD; PAL; PAM; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidyl-glycine alpha-amidating monooxygenase; Peptidylamidoglycolate lyase; peptidylglycine alpha-amidating monooxygenase; Peptidylglycine alpha-hydroxylating monooxygenase; PHM
Gene Symbols: Pam
Molecular weight: 108,675 Da
Basal Isoelectric point: 5.78  Predict pI for various phosphorylation states
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PAM

Protein Structure Not Found.


Cross-references to other databases:  AlphaFold  |  STRING  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene