PROSITE documentation PDOC01038S-adenosylmethionine decarboxylase signature
S-adenosylmethionine decarboxylase (EC 4.1.1.50) (AdoMetDC) [1] 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. | |
| Source | Structure 7:583-595(1999). | |
| PubMed ID | 10378277 |
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 prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)