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We previously had found high expression of PAM in several regions of the developing rodent.
To determine the function of PAM during mouse embryogenesis, we produced a null mutant of the PAM gene.
Recombinant human PAM was expressed as a C-terminally truncated protein lacking its transmembrane and cytosolic domains to facilitate its secretion.
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EC 184.108.40.206: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PHM), 2.Involved in the biosynthesis of alpha-melanotropin and related biologically active peptides.equilibrium-ordered and steady-state-random or -ordered reaction mechanism for the wild-type and the mutant Y318F enzyme, respectively, active site Y318 is involved, C-H bond activation is dominated by quantum mechanical tunneling, peptide substrate binding structure at the active site detailed analysis of the reaction mechanism, reaction scheme, strictly ordered ping-pong kinetic mechanism in which ascorbate first reduces Cu(II) to Cu(I), semidehydroascorbate being released, after which the peptide binds and finally oxygen, active site structure A copper protein.Pedptidylglycine alpha -Amidating Monooxygenase (PAM) catalyzes the C-terminal amidation that is required for the function of a number of peptide hormones (1).PAM possesses two enzymatic activities on a single polypeptide chain (2), due to the presence of a peptidylglycine alpha ‑hydroxylating monooxygenase (PHM) domain and a peptidyl‑ alpha ‑hydroxyglycine alpha ‑amidating lyase (PAL) domain.Ablation of PAM thus demonstrates an essential function for this gene during mouse development, while alterations in PAM activity in the adult may underlie more subtle physiologic effects.The production of alpha-amidated peptides from their glycine-extended precursors is a two-step process involving the sequential action of two catalytic domains encoded by the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) precursor.This 50-k Da PAL protein was purified and found to begin at Asp434 of b PAM, indicating that it could arise through endoproteolytic cleavage of the b PAM precursor at Lys432-Lys433.With alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine as the substrate, PAL exhibits a p H optimum of 5.0; enzymatic activity is inhibited by high concentrations of salt but is relatively resistant to thiol reagents and urea.Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme.Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.