KEGG   ENZYME: 2.5.1.23Help
Entry
EC 2.5.1.23                 Enzyme                                 

Name
sym-norspermidine synthase;
S-adenosylmethioninamine:propane-1,3-diamine 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)
BRITE hierarchy
Sysname
S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase
Reaction(IUBMB)
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-thioadenosine + bis(3-aminopropyl)amine [RN:R03271]
Reaction(KEGG)
Substrate
S-adenosyl 3-(methylthio)propylamine [CPD:C01137];
propane-1,3-diamine [CPD:C00986]
Product
S-methyl-thioadenosine;
bis(3-aminopropyl)amine [CPD:C03375]
Comment
The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylthio)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency [3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase).
History
EC 2.5.1.23 created 1983, modified 2013
Reference
1  [PMID:116684]
  Authors
Aleksijevic A, Grove J, Schuber F.
  Title
Studies on polyamine biosynthesis in Euglena gracilis.
  Journal
Biochim. Biophys. Acta. 565 (1979) 199-207.
Reference
2
  Authors
Villanueva, V.R., Adlakha, R.C. and Calbayrac, R.
  Title
Biosynthesis of polyamines in Euglena gracilis.
  Journal
Phytochemistry 19 (1980) 787-790.
Reference
3  [PMID:3096734]
  Authors
Cacciapuoti G, Porcelli M, Carteni-Farina M, Gambacorta A, Zappia V
  Title
Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium.
  Journal
Eur. J. Biochem. 161 (1986) 263-71.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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