1 Contains
DB identifier | Type | Name |
---|---|---|
IPR018166 | Conserved_site | S-adenosylmethionine decarboxylase, conserved site |
Type: | Family | Name: | S-adenosylmethionine decarboxylase subgroup |
Description: | S-adenosylmethionine decarboxylase (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, 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. | Short Name: | S-AdoMet_decarboxylase_subgr |
DB identifier | Type | Name |
---|---|---|
IPR018166 | Conserved_site | S-adenosylmethionine decarboxylase, conserved site |