The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.5.1.23     
Accepted name: sym-norspermidine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + propane-1,3-diamine = S-methyl-5′-thioadenosine + bis(3-aminopropyl)amine
Glossary: S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): S-adenosylmethioninamine:propane-1,3-diamine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:propane-1,3-diamine 3-aminopropyltransferase
Comments: 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-(methylsulfanyl)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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Aleksijevic, A., Grove, J. and Schuber, F. Studies on polyamine biosynthesis in Euglena gracilis. Biochim. Biophys. Acta 565 (1979) 199–207. [DOI] [PMID: 116684]
2.  Villanueva, V.R., Adlakha, R.C. and Calbayrac, R. Biosynthesis of polyamines in Euglena gracilis. Phytochemistry 19 (1980) 787–790.
3.  Cacciapuoti, G., Porcelli, M., Carteni-Farina, M., Gambacorta, A. and Zappia, V. Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. Eur. J. Biochem. 161 (1986) 263–271. [DOI] [PMID: 3096734]
[EC 2.5.1.23 created 1983, modified 2013]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald