Start Amidating enzyme

Amidating enzyme

Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed. Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides.

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In vertebrates, peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional protein found in secretory granules.

We used well-established enzymatic assays specific for the peptidylglycine-α -hydroxylating monooxygenase (PHM) and peptidyl-α-hydroxyglycine α-amidating lyase (PAL) domains of PAM to quantify amidating activity in the sera of 144 elderly men.

Relationships between PHM and PAL activity and serum levels of their respective active-site metals, Cu and Zn, were analyzed.

Drosophila PHM encodes an active enzyme that is required for peptide amidation in vivo [PMID: 10993678], while both PAL proteins display PAL enzymatic activity and are involved in neuroendocrine biosynthesis [PMID: 15198673].

Background: Peptidylglycine alpha-Amidating Monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important post-translational modification.

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of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced. This subsection of the ‘Subcellular location’ section describes the extent of a membrane-spanning region of the protein.