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Many bioactive peptides must be amidated to exhibit full activity. In peptide hormones, amidation is a common posttranslational modification (PTM) that is mediated in a two-step process by the hydroxylase and lyase activities of the bifunctional enzyme, peptidylglycine alpha-amidation monooxygenase (Driscoll et al., 1999). Amidation had also been reported involved in a variety of pathological processes such as neural dysfunction (Bousquet-Moore et al., 2010), sleep apnea (Kuyama et al., 2009), cancer (Dennison et al., 2009; Rocchi et al., 2001), and hypertension (Shimosawa et al., 2000).
(Bousquet-Moore et al., 2010) Interactions of peptide amidation and copper: novel biomarkers and mechanisms of neural dysfunction. Neurobiol Dis.
(Dennison et al., 2009) The effect of C-terminal amidation on the efficacy and selectivity of antimicrobial and anticancer peptides. Mol Cell Biochem.
(Driscoll et al., 1999) Differential regulation of peptide α-amidation by dexamethasone and disulfiram. Mol Pharmacol.
(Kuyama et al., 2009) A new approach for detecting C-terminal amidation of proteins and peptides by mass spectrometry in conjunction with chemical derivatization. Proteomics.
(Rocchi et al., 2001) Expression of adrenomedullin and peptide amidation activity in human prostate cancer and in human prostate cancer cell lines. Cancer Res.
(Shimosawa et al., 2000) Adrenomedullin amidation enzyme activities in hypertensive patients. Hypertens Res.
(Wang et al., 2017) PrAS: Prediction of amidation sites using multiple feature extraction. Comput Biol Chem.