Anti-Human PAM Antibody Pair

Product Description: Peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional enzyme crucial for the biosynthesis of many signaling peptides and fatty acid amides. It catalyzes the conversion of peptides with a C-terminal glycine into peptides with a terminal amide group, a process essential for the bioactivity of these peptides. PAM has two enzymatically active domains: peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). The PHM domain hydroxylates the C-terminal glycine residue using a copper ion cofactor and oxygen, while the PAL domain completes the conversion by eliminating glyoxylate from the hydroxylated glycine, producing the alpha-amidated peptide. This enzyme is encoded by the PAM gene in humans and is expressed in various endocrine and exocrine glands. The transformation makes peptides more hydrophobic and neutrally charged, enhancing their ability to bind to receptors. Protein Function: 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) [The Uniprot Consortium]