Our results characterize large variation in serum amidating activity and provide unique insight into its potential origin and determinants.
Common non-coding polymorphisms affect serum amidating activity and Cu levels.
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.
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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conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological p H by peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PHL) at alkaline p H spontaneous conversion; EC 126.96.36.199 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1.
Study subjects possessing the minor alleles for rs32680 had lower PHM and PAL activities, and subjects with minor alleles for rs11952361 and rs10515341 had lower PHM activities.
These defects include thinning of the aorta and carotid arteries and are very similar to those of the recently characterized adrenomedullin (AM) gene KO despite the presence of elevated immunoreactive AM in PAM KO embryos.
No peptide amidation activity was detected in PAM mutant embryos, and there was no moderation of the AM-like phenotype that could be expected if any alternative peptide amidation mechanism exists in the mouse.
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