PAM
Description
The PAM (peptidylglycine alpha-amidating monooxygenase) is a protein-coding gene located on chromosome 5.
PAM or PAM may refer to:
PAM (Peptidyl-glycine alpha-amidating monooxygenase) is a bifunctional enzyme responsible for the post-translational modification of inactive peptidylglycine precursors into bioactive alpha-amidated peptides, a crucial step in the biosynthesis of various neural and endocrine peptides. This process involves two sequential reactions catalyzed by separate domains of the enzyme. The first step, catalyzed by the peptidyl alpha-hydroxylating monooxygenase (PHM) domain, requires copper, ascorbate, and oxygen to perform a stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine in the peptidylglycine substrate. The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, utilizes zinc to cleave the N-C-alpha bond, resulting in the formation of the alpha-amidated peptide and glyoxylate. Notably, PAM also catalyzes the conversion of an N-fatty acylglycine into a primary fatty acid amide and glyoxylate.
PAM is also known as PAL, PAM-1, PHM.
