KEGG   ENZYME: 1.5.3.13Help
Entry
EC 1.5.3.13                 Enzyme                                 

Name
N1-acetylpolyamine oxidase;
hPAO-1;
PAO (ambiguous);
mPAO;
hPAO;
polyamine oxidase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)
Reaction(IUBMB)
(1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 [RN:R09074];
(2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 [RN:R03899]
Reaction(KEGG)
Substrate
N1-acetylspermidine [CPD:C00612];
O2 [CPD:C00007];
H2O [CPD:C00001];
N1-acetylspermine [CPD:C02567]
Product
putrescine [CPD:C00134];
3-acetamidopropanal [CPD:C18170];
H2O2 [CPD:C00027];
spermidine [CPD:C00315]
Comment
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).
History
EC 1.5.3.13 created 2009
Orthology
K00308  N1-acetylpolyamine oxidase
Genes
HSA: 196743(PAOX)
PTR: 100612198(PAOX)
PPS: 100991166(PAOX)
GGO: 101144152(PAOX)
PON: 100447841(PAOX)
NLE: 100591252(PAOX)
MCC: 100498675(PAOX)
MCF: 102133238(PAOX)
CSAB: 103245972(PAOX)
RRO: 104677646(PAOX)
RBB: 108543375(PAOX)
CJC: 100391148(PAOX)
SBQ: 101035835(PAOX)
MMU: 212503(Paox)
RNO: 293589(Paox)
CGE: 100754371(Paox)
NGI: 103725840(Paox)
HGL: 101697041(Paox)
CCAN: 109698400(Paox)
OCU: 100341296(PAOX)
TUP: 102487097(PAOX)
AML: 100470303(PAOX)
UMR: 103659644(PAOX)
ORO: 101366439(PAOX)
FCA: 101090142(PAOX)
PTG: 102954249(PAOX)
BTA: 282639(PAOX)
BOM: 102280842(PAOX)
BIU: 109553024(PAOX)
PHD: 102327990(PAOX)
CHX: 102185531(PAOX)
OAS: 101111594(PAOX)
SSC: 100626281(PAOX)
CFR: 102509887(PAOX)
CDK: 105104593(PAOX)
BACU: 103020663(PAOX)
LVE: 103087537(PAOX)
OOR: 101276665(PAOX)
ECB: 100629322(PAOX)
EPZ: 103545896 103556402(PAOX)
EAI: 106841087(PAOX)
MYD: 102769158(PAOX)
HAI: 109383553(PAOX)
RSS: 109445719(PAOX)
PALE: 102897106(PAOX)
LAV: 100671217(PAOX)
TMU: 101340288
MDO: 100618593(PAOX)
SHR: 100935074(PAOX)
OAA: 100091298
GGA: 100857693(PAOX)
CJO: 107315627(PAOX)
APLA: 101801843(PAOX)
ACYG: 106030647(PAOX)
TGU: 100226026(PAOX)
FAB: 101813552(PAOX)
PHI: 102109800 106628584(PAOX)
PMAJ: 107207134(PAOX)
CCAE: 111944263
FPG: 101915114(PAOX)
FCH: 102054181(PAOX)
CLV: 102084101(PAOX)
EGZ: 104125146(PAOX)
AAM: 106495312(PAOX)
ASN: 102375090(PAOX)
AMJ: 102575603(PAOX)
PSS: 102444520(PAOX)
CMY: 102934388(PAOX)
CPIC: 101935511(PAOX)
ACS: 100563036(paox)
PVT: 110087238(PAOX)
PBI: 103061034(PAOX)
GJA: 107106972(PAOX)
XLA: 108701271 495472(paox.L)
XTR: 496840(paox)
NPR: 108792302 108793155(PAOX)
DRE: 562105(si:dkey-275b16.2)
IPU: 108263770(paox)
AMEX: 103029926(paox)
TRU: 101066188 101066416(paox)
LCO: 104924262 109138671(paox)
NCC: 104961348(paox)
NFU: 107375621(paox) 107375622
KMR: 108234132(paox)
CSEM: 103387348(paox)
LCF: 108888274 108888275(paox)
HCQ: 109516209(paox)
BPEC: 110157178(paox)
SASA: 106576873(paox)
OTW: 112252755(paox)
ELS: 105010685(paox)
SFM: 108918131(paox)
LCM: 102353427(PAOX)
CMK: 103178487 103182165(paox)
SPU: 579633
 » show all
Taxonomy
Reference
1  [PMID:12477380]
  Authors
Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW
  Title
Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion.
  Journal
Biochem J 370:19-28 (2003)
DOI:10.1042/BJ20021779
  Sequence
[hsa:196743]
Reference
2  [PMID:15611107]
  Authors
Jarvinen A, Grigorenko N, Khomutov AR, Hyvonen MT, Uimari A, Vepsalainen J, Sinervirta R, Keinanen TA, Vujcic S, Alhonen L, Porter CW, Janne J
  Title
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.
  Journal
J Biol Chem 280:6595-601 (2005)
DOI:10.1074/jbc.M412788200
Reference
3  [PMID:15791459]
  Authors
Wang Y, Hacker A, Murray-Stewart T, Frydman B, Valasinas A, Fraser AV, Woster PM, Casero RA Jr
  Title
Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity.
  Journal
Cancer Chemother Pharmacol 56:83-90 (2005)
DOI:10.1007/s00280-004-0936-5
Reference
4  [PMID:12660232]
  Authors
Wu T, Yankovskaya V, McIntire WS
  Title
Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase.
  Journal
J Biol Chem 278:20514-25 (2003)
DOI:10.1074/jbc.M302149200
  Sequence
[mmu:212503]
Other DBs
ExplorEnz - The Enzyme Database: 1.5.3.13
IUBMB Enzyme Nomenclature: 1.5.3.13
ExPASy - ENZYME nomenclature database: 1.5.3.13
BRENDA, the Enzyme Database: 1.5.3.13

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