The Enzyme Database

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EC 1.4.3.4     
Accepted name: monoamine oxidase
Reaction: RCH2NHR′ + H2O + O2 = RCHO + R′NH2 + H2O2
Other name(s): adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; MAO; MAO A; MAO B; MAO-A; MAO-B; monoamine oxidase A; monoamine oxidase B; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase
Systematic name: amine:oxygen oxidoreductase (deaminating)
Comments: A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines [3]. Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9001-66-5
References:
1.  Blaschko, H. Amine oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 337–351.
2.  Dostert, P.L., Strolin Benedetti, M. and Tipton, K.F. Interactions of monoamine oxidase with substrates and inhibitors. Med. Res. Rev. 9 (1989) 45–89. [DOI] [PMID: 2644497]
3.  Edmondson, D.E., Mattevi, A., Binda, C., Li, M. and Hubálek, F. Structure and mechanism of monoamine oxidase. Curr. Med. Chem. 11 (2004) 1983–1993. [PMID: 15279562]
4.  Shih, J.C. and Chen, K. Regulation of MAO-A and MAO-B gene expression. Curr. Med. Chem. 11 (2004) 1995–2005. [PMID: 15279563]
5.  Tipton, K.F., Boyce, S., O'Sullivan, J., Davey, G.P. and Healy, J. Monoamine oxidases: certainties and uncertainties. Curr. Med. Chem. 11 (2004) 1965–1982. [PMID: 15279561]
6.  De Colibus, L., Li, M., Binda, C., Lustig, A., Edmondson, D.E. and Mattevi, A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl. Acad. Sci. USA 102 (2005) 12684–12689. [DOI] [PMID: 16129825]
7.  Youdim, M.B., Edmondson, D. and Tipton, K.F. The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. 7 (2006) 295–309. [DOI] [PMID: 16552415]
8.  Youdim, M.B. and Bakhle, Y.S. Monoamine oxidase: isoforms and inhibitors in Parkinson′s disease and depressive illness. Br. J. Pharmacol. 147 Suppl. 1 (2006) S287–S296. [DOI] [PMID: 16402116]
[EC 1.4.3.4 created 1961, modified 1983 (EC 1.4.3.9 created 1972, incorporated 1984), modified 2008]
 
 
EC 1.5.1.43     
Accepted name: carboxynorspermidine synthase
Reaction: (1) carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
(2) carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+
Other name(s): carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name)
Systematic name: carboxynorspermidine:NADP+ oxidoreductase
Comments: The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively [1]. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation [2]. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nakao, H., Shinoda, S. and Yamamoto, S. Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus. J. Gen. Microbiol. 137 (1991) 1737–1742. [DOI] [PMID: 1955861]
2.  Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899–9907. [DOI] [PMID: 19196710]
3.  Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286 (2011) 43301–43312. [DOI] [PMID: 22025614]
[EC 1.5.1.43 created 2012]
 
 
EC 1.5.3.11      
Deleted entry: polyamine oxidase. Now included with EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase)
[EC 1.5.3.11 created 1992, deleted 2009]
 
 
EC 1.5.3.13     
Accepted name: N1-acetylpolyamine oxidase
Reaction: (1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
(2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
Other name(s): hPAO-1; PAO (ambiguous); mPAO; hPAO; polyamine oxidase (ambiguous)
Systematic name: N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)
Comments: The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vujcic, S., Liang, P., Diegelman, P., Kramer, D.L. and Porter, C.W. Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem. J. 370 (2003) 19–28. [DOI] [PMID: 12477380]
2.  Jarvinen, A., Grigorenko, N., Khomutov, A.R., Hyvonen, M.T., Uimari, A., Vepsalainen, J., Sinervirta, R., Keinanen, T.A., Vujcic, S., Alhonen, L., Porter, C.W. and Janne, J. Metabolic stability of α-methylated polyamine derivatives and their use as substitutes for the natural polyamines. J. Biol. Chem. 280 (2005) 6595–6601. [DOI] [PMID: 15611107]
3.  Wang, Y., Hacker, A., Murray-Stewart, T., Frydman, B., Valasinas, A., Fraser, A.V., Woster, P.M. and Casero, R.A., Jr. Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. Cancer Chemother. Pharmacol. 56 (2005) 83–90. [DOI] [PMID: 15791459]
4.  Wu, T., Yankovskaya, V. and McIntire, W.S. Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J. Biol. Chem. 278 (2003) 20514–20525. [DOI] [PMID: 12660232]
[EC 1.5.3.13 created 2009]
 
 
EC 1.5.3.14     
Accepted name: polyamine oxidase (propane-1,3-diamine-forming)
Reaction: spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2
Other name(s): MPAO (ambiguous); maize PAO
Systematic name: spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
Comments: As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tavladoraki, P., Schinina, M.E., Cecconi, F., Di Agostino, S., Manera, F., Rea, G., Mariottini, P., Federico, R. and Angelini, R. Maize polyamine oxidase: primary structure from protein and cDNA sequencing. FEBS Lett. 426 (1998) 62–66. [DOI] [PMID: 9598979]
2.  Federico, R., Ercolini, L., Laurenzi, M., Angelini, R. Oxidation of acetylpolyamines by maize polyamine oxidase. Phytochemistry 43 (1996) 339–341.
[EC 1.5.3.14 created 2009]
 
 
EC 1.5.3.15     
Accepted name: N8-acetylspermidine oxidase (propane-1,3-diamine-forming)
Reaction: N8-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2
Systematic name: N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
Comments: Also active with N1-acetylspermine, weak activity with N1,N12-diacetylspermine. No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase (EC 1.4.3.4) activity. Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shukla, O.P., Muller, S. and Walter, R.D. Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine. Mol. Biochem. Parasitol. 51 (1992) 91–98. [DOI] [PMID: 1565141]
[EC 1.5.3.15 created 2009]
 
 
EC 1.5.3.16     
Accepted name: spermine oxidase
Reaction: spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
Other name(s): PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu
Systematic name: spermidine:oxygen oxidoreductase (spermidine-forming)
Comments: The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Murray-Stewart, T., Wang, Y., Goodwin, A., Hacker, A., Meeker, A. and Casero, R.A., Jr. Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology. FEBS J. 275 (2008) 2795–2806. [DOI] [PMID: 18422650]
2.  Cervelli, M., Polticelli, F., Federico, R. and Mariottini, P. Heterologous expression and characterization of mouse spermine oxidase. J. Biol. Chem. 278 (2003) 5271–5276. [DOI] [PMID: 12458219]
3.  Tavladoraki, P., Rossi, M.N., Saccuti, G., Perez-Amador, M.A., Polticelli, F., Angelini, R. and Federico, R. Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion. Plant Physiol. 141 (2006) 1519–1532. [DOI] [PMID: 16778015]
4.  Wang, Y., Murray-Stewart, T., Devereux, W., Hacker, A., Frydman, B., Woster, P.M. and Casero, R.A., Jr. Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem. Biophys. Res. Commun. 304 (2003) 605–611. [DOI] [PMID: 12727196]
[EC 1.5.3.16 created 2009]
 
 
EC 1.5.3.17     
Accepted name: non-specific polyamine oxidase
Reaction: (1) spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
(2) spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2
(3) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
(4) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
Other name(s): polyamine oxidase (ambiguous); Fms1; AtPAO3
Systematic name: polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)
Comments: A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Moschou, P.N., Sanmartin, M., Andriopoulou, A.H., Rojo, E., Sanchez-Serrano, J.J. and Roubelakis-Angelakis, K.A. Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis. Plant Physiol. 147 (2008) 1845–1857. [DOI] [PMID: 18583528]
2.  Muller, S. and Walter, R.D. Purification and characterization of polyamine oxidase from Ascaris suum. Biochem. J. 283 (1992) 75–80. [PMID: 1567380]
3.  Landry, J. and Sternglanz, R. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem. Biophys. Res. Commun. 303 (2003) 771–776. [DOI] [PMID: 12670477]
[EC 1.5.3.17 created 2009]
 
 
EC 1.5.99.6     
Accepted name: spermidine dehydrogenase
Reaction: spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal + reduced acceptor
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
Other name(s): spermidine:(acceptor) oxidoreductase
Systematic name: spermidine:acceptor oxidoreductase
Comments: A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-64-6
References:
1.  Tabor, C.W. and Kellogg, P.D. Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens. J. Biol. Chem. 245 (1970) 5424–5433. [PMID: 4918845]
2.  Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 225–226.
[EC 1.5.99.6 created 1976]
 
 
EC 1.8.1.12     
Accepted name: trypanothione-disulfide reductase
Reaction: trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
For diagram of trypanothione biosynthesis, click here
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
trypanothione = N1,N8-bis(glutathionyl)spermidine
Other name(s): trypanothione reductase; NADPH2:trypanothione oxidoreductase
Systematic name: trypanothione:NADP+ oxidoreductase
Comments: Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102210-35-5
References:
1.  Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 25 (1986) 3519–3526. [PMID: 3718941]
2.  Marsh, I.R. and Bradley, M. Substrate specificity of trypanothione reductase. Eur. J. Biochem. 243 (1977) 690–694. [DOI] [PMID: 9057833]
3.  Cunningham, M.L. and Fairlamb, A.H. Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials. Eur. J. Biochem. 230 (1995) 460–468. [DOI] [PMID: 7607216]
[EC 1.8.1.12 created 1989 as EC 1.6.4.8, transferred 2002 to EC 1.8.1.12]
 
 
EC 2.3.1.57     
Accepted name: diamine N-acetyltransferase
Reaction: acetyl-CoA + an alkane-α,ω-diamine = CoA + an N-acetyldiamine
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
Other name(s): spermidine acetyltransferase; putrescine acetyltransferase; putrescine (diamine)-acetylating enzyme; diamine acetyltransferase; spermidine/spermine N1-acetyltransferase; spermidine N1-acetyltransferase; acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase; putrescine acetylase; putrescine N-acetyltransferase
Systematic name: acetyl-CoA:alkane-α,ω-diamine N-acetyltransferase
Comments: Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54596-36-0
References:
1.  Della Ragione, F. and Pegg, A.E. Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver. Biochemistry 21 (1982) 6152–6158. [PMID: 7150547]
[EC 2.3.1.57 created 1976, modified 1989]
 
 
EC 2.3.1.248     
Accepted name: spermidine disinapoyl transferase
Reaction: 2 sinapoyl-CoA + spermidine = 2 CoA + N1,N8-bis(sinapoyl)-spermidine
Other name(s): SDT
Systematic name: sinapoyl-CoA:spermidine N-(hydroxycinnamoyl)transferase
Comments: The enzyme from the plant Arabidopsis thaliana has no activity with 4-coumaroyl-CoA (cf. EC 2.3.1.249, spermidine dicoumaroyl transferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Luo, J., Fuell, C., Parr, A., Hill, L., Bailey, P., Elliott, K., Fairhurst, S.A., Martin, C. and Michael, A.J. A novel polyamine acyltransferase responsible for the accumulation of spermidine conjugates in Arabidopsis seed. Plant Cell 21 (2009) 318–333. [DOI] [PMID: 19168716]
[EC 2.3.1.248 created 2015]
 
 
EC 2.3.1.249     
Accepted name: spermidine dicoumaroyl transferase
Reaction: 2 4-coumaroyl-CoA + spermidine = 2 CoA + N1,N8-bis(4-coumaroyl)-spermidine
Other name(s): SCT
Systematic name: 4-coumaroyl-CoA:spermidine N-(hydroxycinnamoyl)transferase
Comments: The enzyme from the plant Arabidopsis thaliana has no activity with sinapoyl-CoA (cf. EC 2.3.1.248, spermidine disinapoyl transferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Luo, J., Fuell, C., Parr, A., Hill, L., Bailey, P., Elliott, K., Fairhurst, S.A., Martin, C. and Michael, A.J. A novel polyamine acyltransferase responsible for the accumulation of spermidine conjugates in Arabidopsis seed. Plant Cell 21 (2009) 318–333. [DOI] [PMID: 19168716]
[EC 2.3.1.249 created 2015]
 
 
EC 2.5.1.16     
Accepted name: spermidine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5′-thioadenosine + spermidine
For diagram of spermine biosynthesis, click here
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
putrescine = butane-1,4-diamine
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): aminopropyltransferase; putrescine aminopropyltransferase; spermidine synthetase; SpeE (ambiguous); S-adenosylmethioninamine:putrescine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:putrescine 3-aminopropyltransferase
Comments: The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-82-0
References:
1.  Hannonen, P., Janne, J. and Raina, A. Partial purification and characterization of spermine synthase from rat brain. Biochim. Biophys. Acta 289 (1972) 225–231. [DOI] [PMID: 4564056]
2.  Pegg, A.E., Shuttleworth, K. and Hibasami, H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem. J. 197 (1981) 315–320. [PMID: 6798961]
3.  Tabor, C.W. Propylamine transferase (spermidine synthesis). Methods Enzymol. 5 (1962) 761–765.
4.  Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 203–268. [PMID: 4628436]
5.  Bowman, W.H., Tabor, C.W. and Tabor, H. Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli. J. Biol. Chem. 248 (1973) 2480–2486. [PMID: 4572733]
6.  Korolev, S., Ikeguchi, Y., Skarina, T., Beasley, S., Arrowsmith, C., Edwards, A., Joachimiak, A., Pegg, A.E. and Savchenko, A. The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat. Struct. Biol. 9 (2002) 27–31. [DOI] [PMID: 11731804]
7.  Yoon, S.O., Lee, Y.S., Lee, S.H. and Cho, Y.D. Polyamine synthesis in plants: isolation and characterization of spermidine synthase from soybean (Glycine max) axes. Biochim. Biophys. Acta 1475 (2000) 17–26. [DOI] [PMID: 10806333]
[EC 2.5.1.16 created 1972, modified 1982, modified 2013]
 
 
EC 2.5.1.22     
Accepted name: spermine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + spermine
For diagram of spermine biosynthesis, click here
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
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): spermidine aminopropyltransferase; spermine synthetase; S-adenosylmethioninamine:spermidine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase
Comments: The enzyme from mammalia is highly specific for spermidine [2,3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74812-43-4
References:
1.  Hibasami, H., Borchardt, R.T., Chen, S.-Y., Coward, J.K. and Pegg, A.E. Studies of inhibition of rat spermidine synthase and spermine synthase. Biochem. J. 187 (1980) 419–428. [PMID: 7396856]
2.  Pajula, R.-L., Raina, A. and Eloranta, T. Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain. Eur. J. Biochem. 101 (1979) 619–626. [DOI] [PMID: 520313]
3.  Pegg, A.E., Shuttleworth, K. and Hibasami, H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem. J. 197 (1981) 315–320. [PMID: 6798961]
[EC 2.5.1.22 created 1982, modified 2013]
 
 
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
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]
 
 
EC 2.5.1.44     
Accepted name: homospermidine synthase
Reaction: (1) 2 putrescine = sym-homospermidine + NH3 + H+
(2) putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
For diagram of reaction, click here
Glossary: sym-homospermidine = N-(4-aminobutyl)butane-1,4-diamine
putrescine = butane-1,4-diamine
dehydroputrescine = 4-iminobutan-1-amine
Systematic name: putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)
Comments: The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: NAD+-dependent dehydrogenation of putrescine, transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine and reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76106-84-8
References:
1.  Tait, G.H. The formation of homospermidine by an enzyme from Rhodopseudomonas viridis. Biochem. Soc. Trans. 7 (1979) 199–200. [PMID: 437275]
2.  Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80–85.
3.  Yamamoto, S., Nagata, S. and Kusaba, K. Purification and characterization of homospermidine synthase in Acinetobacter tartarogens ATCC 31105. J. Biochem. 114 (1993) 45–49. [PMID: 8407874]
4.  Srivenugopal, K.S. and Adiga, P.R. Enzymatic synthesis of sym-homospermidine in Lathyrus sativus T (grass pea) seedlings. Biochem. J. 190 (1980) 461–464. [PMID: 7470060]
5.  Ober, D., Tholl, D., Martin, W. and Hartmann, T. Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichia coli. J. Gen. Appl. Microbiol. 42 (1996) 411–419.
6.  Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777–14782. [DOI] [PMID: 10611289]
[EC 2.5.1.44 created 1999, modified 2001]
 
 
EC 2.5.1.45     
Accepted name: homospermidine synthase (spermidine-specific)
Reaction: spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
For diagram of reaction, click here
Glossary: sym-homospermidine = N-(4-aminobutyl)butane-1,4-diamine
putrescine = butane-1,4-diamine
spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
Systematic name: spermidine:putrescine 4-aminobutyltransferase (propane-1,3-diamine-forming)
Comments: The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: (a) NAD+-dependent dehydrogenation of spermidine, (b) transfer of the 4-aminobutylidene group from dehydrospermidine to putrescine and (c) reduction of the imine intermediate to form homospermidine. This enzyme is more specific than EC 2.5.1.44, homospermidine synthase, which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group. Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80–85.
2.  Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777–14782. [DOI] [PMID: 10611289]
3.  Ober, D., Harms, R. and Hartmann, T. Cloning and expression of homospermidine synthase from Senecio vulgaris: a revision. Phytochemistry 55 (2000) 311–316. [PMID: 11117878]
[EC 2.5.1.45 created 2001]
 
 
EC 2.5.1.46     
Accepted name: deoxyhypusine synthase
Reaction: [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction)
(1a) spermidine + NAD+ = dehydrospermidine + NADH
(1b) dehydrospermidine + [enzyme]-lysine = N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine
(1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine = N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine
(1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ = [eIF5A-precursor]-deoxyhypusine + NAD+
For diagram of reaction, click here
Glossary: deoxyhypusine = N6-(4-aminobutyl)-L-lysine
hypusine = N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine
spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
Other name(s): spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming)
Systematic name: [eIF5A-precursor]-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming)
Comments: The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. The reaction occurs in four steps: NAD+-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme; 1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 127069-31-2
References:
1.  Wolff, E.C., Park, M.H. and Folk, J.E. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD+. J. Biol. Chem. 265 (1990) 4793–4799. [PMID: 2108161]
2.  Wolff, E.C., Folk, J.E. and Park, M.H. Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase. J. Biol. Chem. 272 (1997) 15865–15871. [DOI] [PMID: 9188485]
3.  Chen, K.Y. and Liu, A.Y.C. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol. Signals 6 (1997) 105–109. [PMID: 9285092]
4.  Ober, D. and Hartmann, T. Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity. J. Biol. Chem. 274 (1999) 32040–32047. [DOI] [PMID: 10542236]
5.  Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777–14782. [DOI] [PMID: 10611289]
6.  Wolff, E.C. and Park, M.H. Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation. Yeast 15 (1999) 43–50. [DOI] [PMID: 10028184]
7.  Wolff, E.C., Wolff, J. and Park, M.H. Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism. J. Biol. Chem. 275 (2000) 9170–9177. [DOI] [PMID: 10734052]
8.  Joe, Y.A., Wolff, E.C. and Park, M.H. Cloning and expression of human deoxyhypusine synthase cDNA: structure-function studies with the recombinant enzyme and mutant proteins. J. Biol. Chem. 270 (1995) 22386–22392. [DOI] [PMID: 7673224]
9.  Tao, Y. and Chen, K.Y. Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA. J. Biol. Chem. 270 (1995) 23984–23987. [DOI] [PMID: 7592594]
[EC 2.5.1.46 provisional version created 1999 as EC 1.1.1.249 deleted 1999, revised and reinstated 2001 as EC 2.5.1.46]
 
 
EC 2.5.1.79     
Accepted name: thermospermine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + thermospermine + H+
Glossary: thermospermine = N1-[3-(3-aminopropylamino)propyl]butane-1,4-diamine
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): TSPMS; ACL5; SAC51; S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing)
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase (thermospermine forming)
Comments: This plant enzyme is crucial for the proper functioning of xylem vessel elements in the vascular tissues of plants [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Romer, P., Faltermeier, A., Mertins, V., Gedrange, T., Mai, R. and Proff, P. Investigations about N-aminopropyl transferases probably involved in biomineralization. J. Physiol. Pharmacol. 59 Suppl 5 (2008) 27–37. [PMID: 19075322]
2.  Knott, J.M., Romer, P. and Sumper, M. Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine. FEBS Lett. 581 (2007) 3081–3086. [DOI] [PMID: 17560575]
3.  Muniz, L., Minguet, E.G., Singh, S.K., Pesquet, E., Vera-Sirera, F., Moreau-Courtois, C.L., Carbonell, J., Blazquez, M.A. and Tuominen, H. ACAULIS5 controls Arabidopsis xylem specification through the prevention of premature cell death. Development 135 (2008) 2573–2582. [DOI] [PMID: 18599510]
[EC 2.5.1.79 created 2010, modified 2013]
 
 
EC 2.5.1.104     
Accepted name: N1-aminopropylagmatine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5′-thioadenosine + N1-(3-aminopropyl)agmatine
For diagram of spermidine biosynthesis, click here
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): agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE (ambiguous); agmatine aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase
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: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and 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 (2005) 30073–30082. [DOI] [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. and 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 (2007) 6057–6067. [DOI] [PMID: 17545282]
3.  Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991–5001. [DOI] [PMID: 20675472]
4.  Ohnuma, M., Ganbe, T., Terui, Y., Niitsu, M., Sato, T., Tanaka, N., Tamakoshi, M., Samejima, K., Kumasaka, T. and Oshima, T. Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus. J. Mol. Biol. 408 (2011) 971–986. [DOI] [PMID: 21458463]
[EC 2.5.1.104 created 2013]
 
 
EC 2.5.1.126     
Accepted name: norspermine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + norspermidine = S-methyl-5′-thioadenosine + norspermine
Glossary: norspermidine = bis(3-aminopropyl)amine
norspermine = N,N′-bis(3-aminopropyl)-1,3-propanediamine
spermidine = N-(3-aminopropyl)-1,4-butanediamine
thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine
Other name(s): long-chain polyamine synthase (ambiguous)
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:norspermidine 3-aminopropyltransferase
Comments: The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Knott, J.M. Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum. FEBS Lett. 583 (2009) 3519–3524. [DOI] [PMID: 19822146]
[EC 2.5.1.126 created 2014]
 
 
EC 2.5.1.127     
Accepted name: caldopentamine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + norspermine = S-methyl-5′-thioadenosine + caldopentamine
Glossary: caldopentamine = N-(3-aminopropyl)-N′-{3-[(3-aminopropyl)amino]propyl}-1,3-propanediamine
norspermidine = N-(3-aminopropyl)-1,4-butanediamine
norspermine = N,N′-bis(3-aminopropyl)-1,3-propanediamine
spermidine = N-(3-aminopropyl)-1,4-butanediamine
thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine
Other name(s): long-chain polyamine synthase (ambiguous)
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:norspermine 3-aminopropyltransferase
Comments: The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Knott, J.M. Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum. FEBS Lett. 583 (2009) 3519–3524. [DOI] [PMID: 19822146]
[EC 2.5.1.127 created 2014]
 
 
EC 2.5.1.128     
Accepted name: N4-bis(aminopropyl)spermidine synthase
Reaction: 2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine (overall reaction)
(1a) S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + N4-aminopropylspermidine
(1b) S-adenosyl 3-(methylsulfanyl)propylamine + N4-aminopropylspermidine = S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
N4-aminopropylspermidine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
N4-bis(aminopropyl)spermidine = N,N,N′-tris(3-aminopropyl)butane-1,4-diamine
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase [N4-bis(aminopropyl)spermidine synthesizing]
Comments: The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N4-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature. When spermine is used as substrate, the enzyme forms N4-aminopropylspermine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Okada, K., Hidese, R., Fukuda, W., Niitsu, M., Takao, K., Horai, Y., Umezawa, N., Higuchi, T., Oshima, T., Yoshikawa, Y., Imanaka, T. and Fujiwara, S. Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles. J. Bacteriol. 196 (2014) 1866–1876. [DOI] [PMID: 24610711]
[EC 2.5.1.128 created 2014]
 
 
EC 2.6.1.82     
Accepted name: putrescine—2-oxoglutarate transaminase
Reaction: putrescine + 2-oxoglutarate = 1-pyrroline + L-glutamate + H2O (overall reaction)
(1a) putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
(1b) 4-aminobutanal = 1-pyrroline + H2O (spontaneous)
For diagram of arginine catabolism, click here
Glossary: putrescine = butane-1,4-diamine
1-pyrroline = 3,4-dihydro-2H-pyrrole
Other name(s): putrescine-α-ketoglutarate transaminase; YgjG; putrescine:α-ketoglutarate aminotransferase; PAT (ambiguous); putrescine transaminase (ambiguous); putrescine aminotransferase (ambiguous); butane-1,4-diamine:2-oxoglutarate aminotransferase
Systematic name: putrescine:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5′-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which is a substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine—pyruvate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 98982-73-1
References:
1.  Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [DOI] [PMID: 3510672]
2.  Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [DOI] [PMID: 16023116]
3.  Samsonova, N.N., Smirnov, S.V., Altman, I.B. and Ptitsyn, L.R. Molecular cloning and characterization of Escherichia coli K12 ygjG gene. BMC Microbiol. 3 (2003) 2. [DOI] [PMID: 12617754]
[EC 2.6.1.82 created 2006, modified 2017]
 
 
EC 3.5.1.48     
Accepted name: acetylspermidine deacetylase
Reaction: N8-acetylspermidine + H2O = acetate + spermidine
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
Other name(s): N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect); 8-N-acetylspermidine amidohydrolase
Systematic name: N8-acetylspermidine amidohydrolase
Comments: It was initially thought that N1-acetylspermidine was the substrate for this deacetylase reaction [1] but this has since been disproved by Marchant et al. [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67339-07-5
References:
1.  Libby, P.R. Properties of an acetylspermidine deacetylase from rat liver. Arch. Biochem. Biophys. 188 (1978) 360–363. [DOI] [PMID: 28089]
2.  Blankenship, J. Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue. Arch. Biochem. Biophys. 189 (1978) 20–27. [DOI] [PMID: 708044]
3.  Marchant, P., Manneh, V.A. and Blankenship, J. N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase. Biochim. Biophys. Acta 881 (1986) 297–299. [DOI] [PMID: 3955076]
[EC 3.5.1.48 created 1984, modified 2005]
 
 
EC 3.5.1.62     
Accepted name: acetylputrescine deacetylase
Reaction: N-acetylputrescine + H2O = acetate + putrescine
Glossary: putrescine = butane-1,4-diamine
spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
Systematic name: N-acetylputrescine acetylhydrolase
Comments: The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 103679-48-7
References:
1.  Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T. Acetylputrescine deacetylase from Micrococcus luteus K-11. Biochim. Biophys. Acta 882 (1986) 140–142.
[EC 3.5.1.62 created 1989]
 
 
EC 3.5.1.63     
Accepted name: 4-acetamidobutyrate deacetylase
Reaction: 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Systematic name: 4-acetamidobutanoate amidohydrolase
Comments: Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-82-0
References:
1.  Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7–14.
[EC 3.5.1.63 created 1989]
 
 
EC 3.5.1.78     
Accepted name: glutathionylspermidine amidase
Reaction: glutathionylspermidine + H2O = glutathione + spermidine
For diagram of trypanothione biosynthesis, click here
Glossary: spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
Other name(s): glutathionylspermidine amidohydrolase (spermidine-forming)
Systematic name: γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase
Comments: Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 171040-71-4
References:
1.  Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T. Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031–14041. [DOI] [PMID: 7775463]
[EC 3.5.1.78 created 1999]
 
 
EC 3.5.3.24     
Accepted name: N1-aminopropylagmatine ureohydrolase
Reaction: N1-aminopropylagmatine + H2O = spermidine + urea
For diagram of spermidine biosynthesis, click here
Systematic name: N1-aminopropylagmatine amidinohydrolase
Comments: The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and 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 (2005) 30073–30082. [DOI] [PMID: 15983049]
2.  Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991–5001. [DOI] [PMID: 20675472]
[EC 3.5.3.24 created 2013]
 
 
EC 3.6.3.31      
Transferred entry: polyamine-transporting ATPase. Now EC 7.6.2.11, polyamine-transporting ATPase
[EC 3.6.3.31 created 2000, deleted 2018]
 
 
EC 4.1.1.50     
Accepted name: adenosylmethionine decarboxylase
Reaction: S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
For diagram of spermidine biosynthesis, click here and for diagram of spermine biosynthesis, click here
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-adenosylmethionine decarboxylase; S-adenosyl-L-methionine decarboxylase; S-adenosyl-L-methionine carboxy-lyase; S-adenosyl-L-methionine carboxy-lyase [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming]
Systematic name: S-adenosyl-L-methionine carboxy-lyase [S-adenosyl 3-(methylsulfanyl)propylamine-forming]
Comments: The Escherichia coli enzyme contains a pyruvoyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9036-20-8
References:
1.  Anton, D.L. and Kutny, R. Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences. J. Biol. Chem. 262 (1987) 2817–2822. [PMID: 3546296]
2.  Tabor, C.W. Adenosylmethionine decarboxylase. Methods Enzymol. 5 (1962) 756–760.
[EC 4.1.1.50 created 1972]
 
 
EC 4.1.1.96     
Accepted name: carboxynorspermidine decarboxylase
Reaction: (1) carboxynorspermidine = bis(3-aminopropyl)amine + CO2
(2) carboxyspermidine = spermidine + CO2
Glossary: bis(3-aminopropyl)amine = norspermidine
Other name(s): carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name)
Systematic name: carboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming)
Comments: A pyridoxal 5′-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae [1]. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899–9907. [DOI] [PMID: 19196710]
2.  Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J. and Phillips, M.A. Evolution of substrate specificity within a diverse family of β/α-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine. J. Biol. Chem. 285 (2010) 25708–25719. [DOI] [PMID: 20534592]
3.  Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286 (2011) 43301–43312. [DOI] [PMID: 22025614]
[EC 4.1.1.96 created 2012]
 
 
EC 6.3.1.8     
Accepted name: glutathionylspermidine synthase
Reaction: glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate
For diagram of trypanothione biosynthesis, click here and for diagram of trypanothione biosynthesis, click here
Glossary: glutathione = γ-L-glutamyl-L-cysteinyl-glycine
spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine
Other name(s): glutathione:spermidine ligase (ADP-forming)
Systematic name: γ-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]
Comments: Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-09-2
References:
1.  Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H. Purification of glutathionylspermidine and trypanothione synthase from Crithidia fasciculata. Protein Sci. 1 (1992) 874–883. [DOI] [PMID: 1304372]
2.  Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T. Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031–14041. [DOI] [PMID: 7775463]
[EC 6.3.1.8 created 1999]
 
 
EC 6.3.1.9     
Accepted name: trypanothione synthase
Reaction: (1) glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate
(2) glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate
For diagram of trypanothione biosynthesis, click here and for diagram of trypanothione biosynthesis, click here
Glossary: N1,N8-bis(glutathionyl)spermidine = trypanothione
Other name(s): glutathionylspermidine:glutathione ligase (ADP-forming)
Systematic name: spermidine/glutathionylspermidine:glutathione ligase (ADP-forming)
Comments: The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyses two subsequent reactions, leading to production of trypanothione from glutathione and spermidine. Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 6.3.1.8, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 3.5.1.78, glutathionylspermidine amidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 130246-69-4
References:
1.  Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H. Purification of glutathionylspermidine and trypanothione synthase from Crithidia fasciculata. Protein Sci. 1 (1992) 874–883. [DOI] [PMID: 1304372]
2.  Oza, S.L., Tetaud, E., Ariyanayagam, M.R., Warnon, S.S. and Fairlamb, A.H. A single enzyme catalyses formation of trypanothione from glutathione and spermidine in Trypanosoma cruzi. J. Biol. Chem. 277 (2002) 35853–35861. [DOI] [PMID: 12121990]
3.  Comini, M., Menge, U., Wissing, J. and Flohe, L. Trypanothione synthesis in crithidia revisited. J. Biol. Chem. 280 (2005) 6850–6860. [DOI] [PMID: 15537651]
4.  Oza, S.L., Shaw, M.P., Wyllie, S. and Fairlamb, A.H. Trypanothione biosynthesis in Leishmania major. Mol. Biochem. Parasitol. 139 (2005) 107–116. [DOI] [PMID: 15610825]
5.  Fyfe, P.K., Oza, S.L., Fairlamb, A.H. and Hunter, W.N. Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. J. Biol. Chem. 283 (2008) 17672–17680. [DOI] [PMID: 18420578]
[EC 6.3.1.9 created 1999, modified 2014]
 
 
EC 7.6.2.11     
Accepted name: ABC-type polyamine transporter
Reaction: ATP + H2O + polyamine-[polyamine-binding protein][side 1] = ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Other name(s): polyamine ABC transporter; polyamine-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, polyamine-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine. In Escherichia coli the enzyme imports spermidine preferentially.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kashiwagi, K., Miyamoto, S., Nukui, E., Kobayashi, H. and Igarashi, K. Functions of potA and potD proteins in spermidine - preferential uptake system in Escherichia coli. J. Biol. Chem. 268 (1993) 19358–19363. [PMID: 8366082]
2.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.6.2.11 created 2000 as EC 3.6.3.31, transferred 2018 to EC 7.6.2.11]
 
 


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