FunctionBifunctional 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. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Sequence similaritiesIn the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family. In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family. Contains 5 NHL repeats.
Cellular localizationMembrane and Secreted. Secreted from secretory granules.