Enzyme

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     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.3 With oxygen as acceptor
ID:1.5.3.17
Description:Non-specific polyamine oxidase.
Alternative Name: Polyamine oxidase.
Cath: 3.50.50.60; 3.90.660.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.3.17
BRENDA Enzyme Link: BRENDA 1.5.3.17
KEGG Enzyme Link: KEGG1.5.3.17
BioCyc Enzyme Link: BioCyc 1.5.3.17
ExPASy Enzyme Link: ExPASy1.5.3.17
EC2PDB Enzyme Link: EC2PDB 1.5.3.17
ExplorEnz Enzyme Link: ExplorEnz 1.5.3.17
PRIAM enzyme-specific profiles Link: PRIAM 1.5.3.17
IntEnz Enzyme Link: IntEnz 1.5.3.17
MEDLINE Enzyme Link: MEDLINE 1.5.3.17
MSA:

1.5.3.17;

Phylogenetic Tree:

1.5.3.17;

Uniprot:
M-CSA:
RHEA:25800 H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 + spermidine
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[CH;+0:2]=[O;H0;+0:7].[*:4]-[NH2;+0:3].[OH;+0:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis.Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA2008 Aug18583528
Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion.Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R2006 Aug16778015
Crystal structures of Fms1 and its complex with spermine reveal substrate specificity.Huang Q, Liu Q, Hao Q2005 May 1315843025
Purification and characterization of polyamine oxidase from Ascaris suum.Müller S, Walter RD1992 Apr 11567380
Yeast Fms1 is a FAD-utilizing polyamine oxidase.Landry J, Sternglanz R2003 Apr 1112670477
Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase.Wu T, Yankovskaya V, McIntire WS2003 Jun 612660232
Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion.Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW2003 Feb 1512477380

RHEA:25804 H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[CH;+0:2]=[O;H0;+0:7].[*:4]-[NH2;+0:3].[OH;+0:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana.Kamada-Nobusada T, Hayashi M, Fukazawa M, Sakakibara H, Nishimura M2008 Sep18703589
Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis.Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA2008 Aug18583528
Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology.Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA Jr2008 Jun18422650
Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion.Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R2006 Aug16778015
Purification and characterization of polyamine oxidase from Ascaris suum.Müller S, Walter RD1992 Apr 11567380
Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA Jr2003 May 1612727196
Yeast Fms1 is a FAD-utilizing polyamine oxidase.Landry J, Sternglanz R2003 Apr 1112670477
Heterologous expression and characterization of mouse spermine oxidase.Cervelli M, Polticelli F, Federico R, Mariottini P2003 Feb 1412458219
Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics.Murray-Stewart T, Wang Y, Devereux W, Casero RA Jr2002 Dec 1512398765
Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin.Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW2002 Nov 112141946

RHEA:25808 H2O + O2 + spermidine = 3-aminopropanal + H2O2 + putrescine
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[CH;+0:2]=[O;H0;+0:7].[*:4]-[NH2;+0:3].[OH;+0:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis.Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA2008 Aug18583528
Purification and characterization of polyamine oxidase from Ascaris suum.Müller S, Walter RD1992 Apr 11567380
Yeast Fms1 is a FAD-utilizing polyamine oxidase.Landry J, Sternglanz R2003 Apr 1112670477
Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics.Murray-Stewart T, Wang Y, Devereux W, Casero RA Jr2002 Dec 1512398765
Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin.Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW2002 Nov 112141946
Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure.Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA Jr2001 Jul 1511454677

RHEA:25812 H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2 + putrescine
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[CH;+0:2]=[O;H0;+0:7].[*:4]-[NH2;+0:3].[OH;+0:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis.Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA2008 Aug18583528
Biochemistry of mammalian peroxisomes revisited.Wanders RJ, Waterham HR200616756494
Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity.Wang Y, Hacker A, Murray-Stewart T, Frydman B, Valasinas A, Fraser AV, Woster PM, Casero RA Jr2005 Jul15791459
Purification and characterization of polyamine oxidase from Ascaris suum.Müller S, Walter RD1992 Apr 11567380
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.Järvinen A, Grigorenko N, Khomutov AR, Hyvönen MT, Uimari A, Vepsäläinen J, Sinervirta R, Keinänen TA, Vujcic S, Alhonen L, Porter CW, Jänne J2005 Feb 2515611107
Yeast Fms1 is a FAD-utilizing polyamine oxidase.Landry J, Sternglanz R2003 Apr 1112670477
Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase.Wu T, Yankovskaya V, McIntire WS2003 Jun 612660232
Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion.Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW2003 Feb 1512477380

RHEA:25972 H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 + propane-1,3-diamine
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[CH;+0:2]=[O;H0;+0:7].[*:4]-[NH2;+0:3].[OH;+0:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine.Shukla OP, Müller S, Walter RD1992 Mar1565141
Yeast Fms1 is a FAD-utilizing polyamine oxidase.Landry J, Sternglanz R2003 Apr 1112670477