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Many neuropeptides and peptide hormones require amidation of their carboxy terminal for full biological activity.

The enzyme peptidyl-α-hydroxyglycine α-amidating lyase (PAL; EC 4.3.2.5) catalyzes the second and last step of this reaction, ) alone and in complex with the nonpeptidic substrate α-hydroxyhippuric acid.

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]. The algorithm is described in the ISO 3309 standard. The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x x 1. In vertebrates, peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional protein found in secretory granules.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.

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