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
| Search

PMC| articles
PubMed| articles
NCBI| proteins
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
| Available protein structures:

Pfam| structures
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary

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

[edit | edit source]

1. ↑ 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.
2. ↑ 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

[edit | edit source]

* Reaction: R00178

This article incorporates text from the public domain Pfam and InterPro: IPR003826

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Carbon-carbon lyases (EC 4.1)

4.1.1: Carboxy-lyases|

* Acetoacetate decarboxylase
* Adenosylmethionine decarboxylase
* Arginine decarboxylase
* Aromatic L-amino acid decarboxylase
* Glutamate decarboxylase
* Histidine decarboxylase
* Lysine decarboxylase
* Malonyl-CoA decarboxylase
* Ornithine decarboxylase
* Oxaloacetate decarboxylase
* Phosphoenolpyruvate carboxykinase
* Phosphoenolpyruvate carboxylase
* Phosphoribosylaminoimidazole carboxylase
* Pyrophosphomevalonate decarboxylase
* Pyruvate decarboxylase
* RuBisCO
* Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase
* Uroporphyrinogen III decarboxylase

4.1.2: Aldehyde-lyases|

* Fructose-bisphosphate aldolase
* Aldolase A
* Aldolase B
* Aldolase C
* 2-hydroxyphytanoyl-CoA lyase
* Threonine aldolase

4.1.3: Oxo-acid-lyases|

* Isocitrate lyase
* 3-hydroxy-3-methylglutaryl-CoA lyase

4.1.99: Other|

* Tryptophanase
* Photolyase
* CPD lyase
* Spore photoproduct lyase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Catalytically perfect enzyme
* Coenzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)

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