The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Richard Cammack, Ron Caspi, Masaaki Kotera, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


Contents

EC 1.5.3.11 deleted
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
EC 1.5.3.17 non-specific polyamine oxidase


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, IUBMB, KEGG
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. [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. [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. [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. [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; 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, IUBMB, KEGG
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. [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, IUBMB, KEGG
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. [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, IUBMB, KEGG
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. [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. [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. [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. [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, IUBMB, KEGG
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. [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. [PMID: 12670477]
[EC 1.5.3.17 created 2009]
 
 


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