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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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 1.5.3.3      
Deleted entry:  spermine oxidase
[EC 1.5.3.3 created 1961, deleted 1972]
 
 
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, PDB
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, PDB
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, PDB
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, PDB
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, PDB
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 = 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, PDB, 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 2.3.1.57     
Accepted name: diamine N-acetyltransferase
Reaction: acetyl-CoA + an alkane-α,ω-diamine = CoA + an N-acetyldiamine
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine.html">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 2.5.1.16     
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 = N-(3-aminopropyl)butane-1,4-diamine
spermine.html">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 = N-(3-aminopropyl)butane-1,4-diamine
spermine.html">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, 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]
 
 
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, PDB
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 2.5.1.126     
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, PDB
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, PDB
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 3.5.1.48     
Accepted name: acetylspermidine deacetylase
Reaction: N8-acetylspermidine + H2O = acetate + spermidine
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine.html">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, PDB, 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 4.1.1.17     
Accepted name: ornithine decarboxylase
Reaction: L-ornithine = putrescine + CO2
For diagram of spermine biosynthesis, click here and for diagram of arginine catabolism, click here
Glossary: putrescine = butane-1,4-diamine
Other name(s): SpeC; L-ornithine carboxy-lyase
Systematic name: L-ornithine carboxy-lyase (putrescine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-60-6
References:
1.  Ono, M., Inoue, H., Suzuki, F. and Takeda, Y. Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats. Purification and some properties. Biochim. Biophys. Acta 284 (1972) 285–297. [DOI] [PMID: 5073764]
2.  Taylor, E.S. and Gale, E.F. Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase content and action of inhibitors. Biochem. J. 39 (1945) 52–58. [PMID: 16747854]
[EC 4.1.1.17 created 1961]
 
 
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. [DOI]
[EC 4.1.1.50 created 1972]
 
 
EC 4.1.1.116     
Accepted name: D-ornithine/D-lysine decarboxylase
Reaction: (1) D-ornithine = putrescine + CO2
(2) D-lysine = cadaverine + CO2
For diagram of spermine biosynthesis, click here
Glossary: cadaverine = pentane-1,5-diamine
putrescine = butane-1,4-diamine
Other name(s): dokD (gene name); DOKDC
Systematic name: D-ornithine/D-lysine carboxy-lyase
Comments: The enzyme, characterized from the bacterium Salmonella typhimurium LT2, is specific for D-ornithine and D-lysine. Requires pyridoxal 5′-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Phillips, R.S., Poteh, P., Miller, K.A. and Hoover, T.R. STM2360 encodes a D-ornithine/D-lysine decarboxylase in Salmonella enterica serovar typhimurium. Arch. Biochem. Biophys. 634 (2017) 83–87. [PMID: 29024617]
[EC 4.1.1.116 created 2019]
 
 
EC 5.1.1.12     
Accepted name: ornithine racemase
Reaction: L-ornithine = D-ornithine
For diagram of spermine biosynthesis, click here
Systematic name: ornithine racemase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-28-9
References:
1.  Chen, H.P., Lin, C.F., Lee, Y.J., Tsay, S.S. and Wu, S.H. Purification and properties of ornithine racemase from Clostridium sticklandii. J. Bacteriol. 182 (2000) 2052–2054. [DOI] [PMID: 10715017]
[EC 5.1.1.12 created 1972 as EC 5.4.3.1, transferred 1976 to EC 5.1.1.12]
 
 


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