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The catalytic core of PHM consists of two β-clamshell or sandwich domains.

In the second step of the reaction, peptidyl-α-hydroxyglycine α-amidating lyase (PAL; EC 4.3.2.5) catalyzes an N-dealkylation reaction, generating amidated product and glyoxylate.Peptidylglycine α-amidating mono-oxygenase is an enzyme found in large dense core vesicles which acts on the final steps of biosynthesis, converting the peptidyl-Gly into the corresponding peptide-NH2.From: The two enzymatic activities necessary to perform the peptide α-amidation reaction are initially synthesized as a single bifunctional precursor protein called peptidylglycine-α-amidating monooxygenase (PAM) (). Alternative splicing generates several forms of PAM that differ in important ways.The Cys residues, which form essential disulfide bridges, are conserved across species.PHM and DBM define a family of copper-dependent monooxygenases that includes at least one additional member, monooxygenase X (MOX), which resembles DBM more closely than PHM.




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