PROSITE documentation PDOC00009Amidation site
The precursor of hormones and other active peptides which are C-terminally amidated is always directly followed [1,2] by a glycine residue which provides the amide group, and most often by at least two consecutive basic residues (Arg or Lys) which generally function as an active peptide precursor cleavage site. Although all amino acids can be amidated, neutral hydrophobic residues such as Val or Phe are good substrates, while charged residues such as Asp or Arg are much less reactive. C-terminal amidation has not yet been shown to occur in unicellular organisms or in plants.
Last update:June 1988 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kreil G. |
| Title | Occurrence, detection, and biosynthesis of carboxy-terminal amides. | |
| Source | Methods Enzymol. 106:218-223(1984). | |
| PubMed ID | 6548541 |
| 2 | Authors | Bradbury A.F. Smyth D.G. |
| Title | Biosynthesis of the C-terminal amide in peptide hormones. | |
| Source | Biosci. Rep. 7:907-916(1987). | |
| PubMed ID | 3331120 |
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