S-adenosylmethionine decarboxylase, core (IPR016067)
Short name: S-AdoMet_deCO2ase_core
- S-adenosylmethionine decarboxylase (IPR001985)
- S-adenosylmethionine decarboxylase family, prokaryotic (IPR003826)
- S-adenosylmethionine decarboxylase, bacterial (IPR009165)
- S-adenosylmethionine decarboxylase proenzyme (IPR017716)
- S-adenosylmethionine decarboxylase, conserved site (IPR018166)
- Arginine decarboxylase proenzyme (IPR027549)
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.
- SSF56276 (SSF56276)