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

S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase

S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-(3-aminopropyl)agmatine [RN:R10338]

R10338
Reaction

S-adenosyl 3-(methylsulfanyl)propylamine [CPD:C01137];
agmatine [CPD:C00179]

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.

EC 2.5.1.104 created 2013

1  [PMID:15983049]

Ohnuma M, Terui Y, Tamakoshi M, Mitome H, Niitsu M, Samejima K, Kawashima E, Oshima T

N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus.

J Biol Chem 280:30073-82 (2005)
DOI:10.1074/jbc.M413332200

[ttj:TTHA0824] [tth:TT_C0472]

2  [PMID:17545282]

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.

The first agmatine/cadaverine aminopropyl transferase: biochemical and structural characterization of an enzyme involved in polyamine biosynthesis in the hyperthermophilic archaeon Pyrococcus furiosus.

J Bacteriol 189:6057-67 (2007)
DOI:10.1128/JB.00151-07

[pfu:PF0127]

3  [PMID:20675472]

Morimoto N, Fukuda W, Nakajima N, Masuda T, Terui Y, Kanai T, Oshima T, Imanaka T, Fujiwara S

Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis.

J Bacteriol 192:4991-5001 (2010)
DOI:10.1128/JB.00279-10

[tko:TK0147]

4  [PMID:21458463]

Ohnuma M, Ganbe T, Terui Y, Niitsu M, Sato T, Tanaka N, Tamakoshi M, Samejima K, Kumasaka T, Oshima T

Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus.

J Mol Biol 408:971-86 (2011)
DOI:10.1016/j.jmb.2011.03.025

[ttj:TTHA0824]