|PROSITE documentation PDOC01038|
S-adenosylmethionine decarboxylase (EC 18.104.22.168) (AdoMetDC)  catalyzes the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines spermidine and spermine from putrescine.
The catalytic mechanism of AdoMetDC involves a covalently-bound pyruvoyl group. This group is post-translationally generated by a self-catalyzed intramolecular proteolytic cleavage reaction between a glutamate and a serine. This cleavage generates two chains, β (N-terminal) and α (C-terminal). The N-terminal serine residue of the α chain is then converted by nonhydrolytic serinolysis into a pyruvyol group.
As a signature pattern for AdoMetDC we selected the region that contains the proteolytic celavage site.Note:
The AdoMetDC enzyme from Escherichia coli does not belong to this family.Last update:
July 1999 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Ekstrom J.L. Mathews I.I. Stanley B.A. Pegg A.E. Ealick S.E.|
|Title||The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold.|