| Post Translational Modifications | Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. |
| Function | Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. |
| Protein Name | S-Adenosylmethionine Decarboxylase ProenzymeAdometdcSamdc Cleaved Into - S-Adenosylmethionine Decarboxylase Alpha Chain - S-Adenosylmethionine Decarboxylase Beta Chain |
| Database Links | Reactome: R-HSA-351202 |
| Alternative Antibody Names | Anti-S-Adenosylmethionine Decarboxylase Proenzyme antibodyAnti-Adometdc antibodyAnti-Samdc Cleaved Into - S-Adenosylmethionine Decarboxylase Alpha Chain - S-Adenosylmethionine Decarboxylase Beta Chain antibodyAnti-AMD1 antibodyAnti-AMD antibody |
Information sourced from Uniprot.org
