Conserved Site

S-adenosylmethionine decarboxylase, conserved site (IPR018166)

Short name: S-AdoMet_deCO2ase_CS


S-adenosylmethionine decarboxylase (AdoMetDC) [PMID: 10378277] 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, beta (N-terminal) and alpha (C-terminal). The N-terminal serine residue of the alpha chain is then converted by nonhydrolytic serinolysis into a pyruvyol group.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004014 adenosylmethionine decarboxylase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns