Enzyme

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EC Tree
     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.3 With oxygen as acceptor
ID:1.5.3.16
Description:Spermine oxidase.
Alternative Name: SMO.
Cath: 3.50.50.60; 3.90.660.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.3.16
BRENDA Enzyme Link: BRENDA 1.5.3.16
KEGG Enzyme Link: KEGG1.5.3.16
BioCyc Enzyme Link: BioCyc 1.5.3.16
ExPASy Enzyme Link: ExPASy1.5.3.16
EC2PDB Enzyme Link: EC2PDB 1.5.3.16
ExplorEnz Enzyme Link: ExplorEnz 1.5.3.16
PRIAM enzyme-specific profiles Link: PRIAM 1.5.3.16
IntEnz Enzyme Link: IntEnz 1.5.3.16
MEDLINE Enzyme Link: MEDLINE 1.5.3.16
MSA:

1.5.3.16;

Phylogenetic Tree:

1.5.3.16;

Uniprot:
M-CSA:
RHEA:25816 H2O + norspermine + O2 = 3-aminopropanal + H2O2 + norspermidine
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
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

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