| adenosylmethionine decarboxylase | |
| Ec Number: | 4.1.1.50 |
| Cas Number: | 9036-20-8 |
| Go Code: | 0004014 |
| adenosylmethionine decarboxylase 1 | |
| Hgncid: | 457 |
| Symbol: | AMD1 |
| Entrezgene: | 262 |
| Omim: | 180980 |
| Refseq: | NM_001634 |
| Uniprot: | P17707 |
| Ecnumber: | 4.1.1.50 |
| Chromosome: | 6 |
| Arm: | q |
| Band: | 21 |
| Locussupplementarydata: | -q22 |
| Symbol: | AdoMet_dc |
| AdoMet decarboxylase | |
| Pfam: | PF02675 |
| Interpro: | IPR003826 |
The enzyme adenosylmethionine decarboxylase catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine.Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in many cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein.[1] [2] Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. In both groups the active enzyme is generated by the post-translational autocatalytic cleavage of a precursor protein. This cleavage generates the pyruvate precursor from an internal serine residue and results in the formation of two non-identical subunits termed alpha and beta which form the active enzyme.