KEGG   ENZYME: 2.5.1.104
Entry
EC 2.5.1.104                Enzyme                                 
Name
N1-aminopropylagmatine synthase;
agmatine/cadaverine aminopropyl transferase;
ACAPT;
PF0127 (gene name);
triamine/agmatine aminopropyltransferase;
SpeE (ambiguous);
agmatine aminopropyltransferase;
S-adenosyl 3-(methylthio)propylamine:agmatine 3-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)
Sysname
S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase
Reaction(IUBMB)
S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-(3-aminopropyl)agmatine [RN:R10338]
Reaction(KEGG)
R10338
Substrate
S-adenosyl 3-(methylsulfanyl)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 280:30073-82 (2005)
DOI:10.1074/jbc.M413332200
  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 189:6057-67 (2007)
DOI:10.1128/JB.00151-07
  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 192:4991-5001 (2010)
DOI:10.1128/JB.00279-10
  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 408:971-86 (2011)
DOI:10.1016/j.jmb.2011.03.025
  Sequence
[ttj:TTHA0824]
Other DBs
ExplorEnz - The Enzyme Database: 2.5.1.104
IUBMB Enzyme Nomenclature: 2.5.1.104
ExPASy - ENZYME nomenclature database: 2.5.1.104
BRENDA, the Enzyme Database: 2.5.1.104

DBGET integrated database retrieval system