Adenosylmethionine decarboxylase
| adenosylmethionine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.1.50 | ||||||||
| CAS number | 9036-20-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| adenosylmethionine decarboxylase 1 | |
|---|---|
| Identifiers | |
| Symbol | AMD1 |
| Entrez | 262 |
| HUGO | 457 |
| OMIM | 180980 |
| RefSeq | NM_001634 |
| UniProt | P17707 |
| Other data | |
| EC number | 4.1.1.50 |
| Locus | Chr. 6 q21-q22 |
| AdoMet decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 1tlu EBI.jpg crystal structure of thermotoga maritima s-adenosylmethionine decarboxylase | |||||||||
| Identifiers | |||||||||
| Symbol | AdoMet_dc | ||||||||
| Pfam | PF02675 | ||||||||
| InterPro | IPR003826 | ||||||||
| |||||||||
Adenosylmethionine decarboxylase is an enzyme that 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 a large number of 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.
References
- ↑ van Poelje PD, Snell EE (1990). "Pyruvoyl-dependent enzymes". Annu. Rev. Biochem. 59: 29–59. doi:10.1146/annurev.bi.59.070190.000333. PMID 2197977.
- ↑ Pegg AE, Xiong H, Feith DJ, Shantz LM (November 1998). "S-adenosylmethionine decarboxylase: structure, function and regulation by polyamines". Biochem. Soc. Trans. 26 (4): 580–6. PMID 10047786.
External links
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