Peptidylglycine alpha amidating

Whereas glycosylation represents the most common modification, additional PTMs, including carboxylation, hydroxylation, sulfation and amidation, are characteristic of some products.

The relationship between structure and function is understood for many PTMs but remains incomplete for others, particularly in the case of complex PTMs, such as glycosylation.

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.

The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part.

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It is the general public with old, wrong information, assumptions and marketing one liners and “naturopathic” rules and anecdotal reports that are insisting on using vitamin C at the wrong dose for the wrong reason. And furthermore Vitamin C needs other nutrients and cofactors (vitamins A, E, D, zinc, and bioflavonoids) in correct balance for it to function at its optimal level. Vitamin c deficiency was found to be the cause of scurvy.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].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. Once cleaved, a propeptide generally has no independent biological function.

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