{PDOC00009}
{PS00009; AMIDATION}
{BEGIN}
******************
* Amidation 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.

-Consensus pattern: x-G-[RK]-[RK]
                    [x is the amidation site]
-Last update: June 1988 / First entry.

[ 1] Kreil G.
     "Occurrence, detection, and biosynthesis of carboxy-terminal amides."
     Methods Enzymol. 106:218-223(1984).
     PubMed=6548541
[ 2] Bradbury A.F., Smyth D.G.
     "Biosynthesis of the C-terminal amide in peptide hormones."
     Biosci. Rep. 7:907-916(1987).
     PubMed=3331120

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}