KEGG   ENZYME: 2.5.1.104Help
Entry
EC 2.5.1.104                Enzyme                                 

Name
N1-aminopropylagmatine synthase;
agmatine/cadaverine aminopropyl transferase;
ACAPT;
PF0127 (gene name);
triamine/agmatine aminopropyltransferase;
SpeE;
agmatine aminopropyltransferase
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase
Reaction(IUBMB)
S-adenosyl 3-(methylthio)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-(3-aminopropyl)agmatine [RN:R10338]
Reaction(KEGG)
Substrate
S-adenosyl 3-(methylthio)propylamine [CPD:C01137];
agmatine [CPD:C00179]
Product
S-methyl-5'-thioadenosine [CPD:C00170];
N1-(3-aminopropyl)agmatine [CPD:C20560]
Comment
The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase.
History
EC 2.5.1.104 created 2013
Reference
1  [PMID:15983049]
  Authors
Ohnuma M, Terui Y, Tamakoshi M, Mitome H, Niitsu M, Samejima K, Kawashima E, Oshima T
  Title
N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus.
  Journal
J. Biol. Chem. 280 (2005) 30073-82.
  Sequence
[ttj:TTHA0824] [tth:TT_C0472]
Reference
2  [PMID:17545282]
  Authors
Cacciapuoti G, Porcelli M, Moretti MA, Sorrentino F, Concilio L, Zappia V, Liu ZJ, Tempel W, Schubot F, Rose JP, Wang BC, Brereton PS, Jenney FE, Adams MW.
  Title
The first agmatine/cadaverine aminopropyl transferase: biochemical and structural characterization of an enzyme involved in polyamine biosynthesis in the hyperthermophilic archaeon Pyrococcus furiosus.
  Journal
J. Bacteriol. 189 (2007) 6057-67.
  Sequence
[pfu:PF0127]
Reference
3  [PMID:20675472]
  Authors
Morimoto N, Fukuda W, Nakajima N, Masuda T, Terui Y, Kanai T, Oshima T, Imanaka T, Fujiwara S
  Title
Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis.
  Journal
J. Bacteriol. 192 (2010) 4991-5001.
  Sequence
[tko:TK0147]
Reference
4  [PMID:21458463]
  Authors
Ohnuma M, Ganbe T, Terui Y, Niitsu M, Sato T, Tanaka N, Tamakoshi M, Samejima K, Kumasaka T, Oshima T
  Title
Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus.
  Journal
J. Mol. Biol. 408 (2011) 971-86.
  Sequence
[ttj:TTHA0824]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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