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The protein contains two enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyse the alpha-amidation of neuroendocrine peptides [PMID: 1988445, PMID: 1448112]: The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide.

The first step of the reaction is catalysed by peptidylglycine alpha-hydroxylating monooxygenase (PHM), and is dependent on copper, ascorbate and molecular oxygen; peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) catalyses the second step of the reaction [PMID: 1448112].

Results: Modification-specific antibodies reveal that peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia.

Conclusion: PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system.

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].

This indicates the type of evidence that supports the existence of the protein.

Interestingly, in Drosophila, the PHM and PAL enzyme are not fused.

Background: Peptidylglycine alpha-Amidating Monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important post-translational modification.Once cleaved, a propeptide generally has no independent biological function. Peptidyl-glycine alpha-amidating monooxygenase is an enzyme that is required for the biosynthesis of many signaling peptides.Ideally this entry shall become one comprehensive and continuous article.Bulleted lists, for instance, were only used because it is impossible to automatically integrate independent facts into a continuous text.




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