EC 2.5.1.104 - N1-aminopropylagmatine synthase

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IntEnz Enzyme Nomenclature
EC 2.5.1.104

Names

Accepted name:
N1-aminopropylagmatine synthase
Other names:
agmatine/cadaverine aminopropyl transferase
ACAPT
PF0127 (gene name)
triamine/agmatine aminopropyltransferase
SpeE
agmatine aminopropyltransferase
Systematic name:
S-3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase

Reaction

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043919 , GO:0043918
UniProtKB/Swiss-Prot:

References

  1. 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: 30073-30082 (2005). [PMID: 15983049]
  2. Cacciapuoti, G., Porcelli, M., Moretti, M. A., Sorrentino, F., Concilio, L., Zappia, V., Liu, Z. J., Tempel, W., Schubot, F., Rose, J. P., Wang, B. C., Brereton, P. S., Jenney, F. E., Adams, M. W.
    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: 6057-6067 (2007). [PMID: 17545282]
  3. 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). [PMID: 20675472]
  4. 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: 971-986 (2011). [PMID: 21458463]

[EC 2.5.1.104 created 2013]