Abstract

Peptidylglycine α-amidating enzyme (α-AE) can be used in an in vitro reaction to convert C-terminal glycine-extended peptides to peptide hormones with a C-terminal amino acid amide. Structure-activity data for 45 bioactive peptides show that the C-terminal amide is required for the full biological activity of most amidated peptide hormones. These data emphasize the role α-AE can have in amidated peptide production.

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