KEGG   ENZYME: 1.5.3.17Help
Entry
EC 1.5.3.17                 Enzyme                                 

Name
non-specific polyamine oxidase;
polyamine oxidase (ambiguous);
Fms1;
AtPAO3
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)
Reaction(IUBMB)
(1) spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2 [RN:R09076];
(2) spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [RN:R09077];
(3) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 [RN:R03899];
(4) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 [RN:R09074]
Reaction(KEGG)
Substrate
spermine [CPD:C00750];
O2 [CPD:C00007];
H2O [CPD:C00001];
spermidine [CPD:C00315];
N1-acetylspermine [CPD:C02567];
N1-acetylspermidine [CPD:C00612]
Product
spermidine [CPD:C00315];
3-aminopropanal [CPD:C05665];
H2O2 [CPD:C00027];
putrescine [CPD:C00134];
3-acetamidopropanal [CPD:C18170]
Comment
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).
History
EC 1.5.3.17 created 2009
Pathway
Arginine and proline metabolism
beta-Alanine metabolism
Orthology
K13367  
polyamine oxidase
K17839  
polyamine oxidase
Genes
ATH: 
AT1G65840(PAO4) AT2G43020(PAO2) AT3G59050(PAO3)
ALY: 
CRB: 
EUS: 
BRP: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0002s05620g(POPTRDRAFT_1071346) POPTR_0004s07430g(POPTRDRAFT_817951) POPTR_0005s22880g(POPTRDRAFT_831582) POPTR_0017s01520g
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os04t0623300-01(Os04g0623300) Os04t0671200-01(Os04g0671200) Os04t0671300-01(Os04g0671300)
OBR: 
BDI: 
SBI: 
SORBI_06g028970(SORBIDRAFT_06g028970) SORBI_06g032450(SORBIDRAFT_06g032450) SORBI_06g032460(SORBIDRAFT_06g032460)
ZMA: 
SITA: 
PDA: 
MUS: 
ATR: 
s00029p00167410(AMTR_s00029p00167410) s00092p00082510(AMTR_s00092p00082510)
SMO: 
PPP: 
SCE: 
YMR020W(FMS1)
AGO: 
ERC: 
KLA: 
LTH: 
ZRO: 
CGR: 
NCS: 
NCAS_0A12730(NCAS0A12730)
NDI: 
NDAI_0B01530(NDAI0B01530)
TDL: 
TDEL_0B06550(TDEL0B06550)
KAF: 
KAFR_0A02140(KAFR0A02140)
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
CLU: 
ZTR: 
PFJ: 
 » show all
Taxonomy
Reference
1  [PMID:18583528]
  Authors
Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA
  Title
Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis.
  Journal
Plant. Physiol. 147 (2008) 1845-57.
  Sequence
[ath:AT3G59050]
Reference
2  [PMID:1567380]
  Authors
Muller S, Walter RD
  Title
Purification and characterization of polyamine oxidase from Ascaris suum.
  Journal
Biochem. J. 283 ( Pt 1) (1992) 75-80.
Reference
3  [PMID:12670477]
  Authors
Landry J, Sternglanz R
  Title
Yeast Fms1 is a FAD-utilizing polyamine oxidase.
  Journal
Biochem. Biophys. Res. Commun. 303 (2003) 771-6.
  Sequence
[sce:YMR020W]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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