EzCatDB: D00042

DB codeD00042
CATH domainDomain 13.50.50.60Catalytic domain
Domain 23.90.660.10Catalytic domain
E.C.1.5.3.14,1.5.3.15
CSA1b5q

CATH domainRelated DB codes (homologues)
3.50.50.60M00163,D00015,D00041,D00045,D00064,D00071,T00004,T00015,T00017,T00025,T00211,T00213,T00233,T00242
3.90.660.10T00211

Enzyme Name
Swiss-protKEGG

O64411
Protein namePolyamine oxidasepolyamine oxidase (propane-1,3-diamine-forming)
   (EC 1.5.3.14)

MPAO
   (EC 1.5.3.14)

maize PAO
   (EC 1.5.3.14)

N8-acetylspermidine oxidase (propane-1,3-diamine-forming)
   (EC 1.5.3.15)

SynonymsEC 1.5.3.n6
EC 1.5.3.n7
EC 1.5.3.n8
EC 1.5.3.n9


Swiss-prot:Accession NumberO64411
Entry namePAO_MAIZE
ActivitySpermidine + O(2) + H(2)O = propane-1,3-diamine + 4-aminobutanal +H(2)O(2).,N(8)-acetylspermidine + O(2) + H(2)O = propane-1,3-diamine + 4-acetamidobutanal + H(2)O(2).,Spermine + O(2) + H(2)O = N-(3-aminopropyl)-4-aminobutanal + trimethylenediamine + H(2)O(2).,N(1)-acetylspermine + O(2) + H(2)O = N-(3-acetamidopropyl)-4-aminobutanal + trimethylenediamine + H(2)O(2).
SubunitMonomer.
Subcellular location
CofactorFAD.


CofactorsSubstratesProductsintermediates
KEGG-idC00016C00001C00007C00315C01029C00027C00986C00555C05936
E.C.
(1.5.3.14, 1.5.3.15)(1.5.3.14, 1.5.3.15)1.5.3.141.5.3.15(1.5.3.14, 1.5.3.15)(1.5.3.14, 1.5.3.15)1.5.3.141.5.3.15
CompoundFADH2OO2spermidineN8-acetylspermidineH2O2propane-1,3-diamine4-aminobutanal4-acetamidobutanal
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideH2Oothersamine group,lipidamide group,amine group,lipidothersamine group,lipidamine group,carbohydrate,lipidamide group,carbohydrate,lipid
1b37A01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b37B01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b37C01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b5qA01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b5qB01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b5qC01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h81A01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h81B01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h81C01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h82A01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h82B01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h82C01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h83A01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h83B01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h83C01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h84A01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h84B01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h84C01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h86A01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h86B01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h86C01Bound:FAD
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b37A02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b37B02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b37C02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b5qA02Unbound
UnboundUnboundAnalogue:MD2UnboundUnboundUnboundUnboundUnbound
1b5qB02Unbound
UnboundUnboundAnalogue:MD2UnboundUnboundUnboundUnboundUnbound
1b5qC02Unbound
UnboundUnboundAnalogue:MD2UnboundUnboundUnboundUnboundUnbound
1h81A02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h81B02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h81C02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1h82A02Unbound
UnboundAnalogue:GZZUnboundUnboundUnboundUnboundUnboundUnbound
1h82B02Unbound
UnboundAnalogue:GZZUnboundUnboundUnboundUnboundUnboundUnbound
1h82C02Unbound
UnboundAnalogue:GZZUnboundUnboundUnboundUnboundUnboundUnbound
1h83A02Unbound
UnboundUnboundUnboundUnboundAnalogue:DIAUnboundUnboundUnbound
1h83B02Unbound
UnboundUnboundUnboundUnboundAnalogue:DIAUnboundUnboundUnbound
1h83C02Unbound
UnboundUnboundUnboundUnboundAnalogue:DIAUnboundUnboundUnbound
1h84A02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:FAD-NBA
1h84B02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:FAD-NBA
1h84C02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:FAD-NBA
1h86A02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:FAD-NBA
1h86B02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:FAD-NBA
1h86C02Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:FAD-NBA

Active-site residues
resource
literature [8]
pdbCatalytic residues
1b37A01GLU 62
1b37B01GLU 62
1b37C01GLU 62
1b5qA01GLU 62
1b5qB01GLU 62
1b5qC01GLU 62
1h81A01GLU 62
1h81B01GLU 62
1h81C01GLU 62
1h82A01GLU 62
1h82B01GLU 62
1h82C01GLU 62
1h83A01GLU 62
1h83B01GLU 62
1h83C01GLU 62
1h84A01GLU 62
1h84B01GLU 62
1h84C01GLU 62
1h86A01GLU 62
1h86B01GLU 62
1h86C01GLU 62
1b37A02GLU 170
1b37B02GLU 170
1b37C02GLU 170
1b5qA02GLU 170
1b5qB02GLU 170
1b5qC02GLU 170
1h81A02GLU 170
1h81B02GLU 170
1h81C02GLU 170
1h82A02GLU 170
1h82B02GLU 170
1h82C02GLU 170
1h83A02GLU 170
1h83B02GLU 170
1h83C02GLU 170
1h84A02GLU 170
1h84B02GLU 170
1h84C02GLU 170
1h86A02GLU 170
1h86B02GLU 170
1h86C02GLU 170

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Fig.1(a), p.271-273
[8]Figure 1p.2767

references
[1]
PubMed ID3181599
JournalInt J Biochem
Year1988
Volume20
Pages695-702
AuthorsTsukada T, Furusako S, Maekawa S, Hibasami H, Nakashima K
TitlePurification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase.
[2]
PubMed ID1654929
JournalBiotechnol Appl Biochem
Year1991
Volume14
Pages54-9
AuthorsCona A, Federico R, Gramiccia M, Orsini S, Gradoni L
TitleThe amino aldehydes produced by spermine and spermidine oxidation with maize polyamine oxidase have anti-leishmanial effect.
[3]
PubMed ID7503806
JournalBiochem Pharmacol
Year1995
Volume50
Pages1527-30
AuthorsLibby PR, Munson BR, Fiel RJ, Porter CW
TitleCationic porphyrin derivatives as inhibitors of polyamine catabolism.
[4]
PubMed ID9210657
JournalArch Biochem Biophys
Year1997
Volume343
Pages146-8
AuthorsBellelli A, Angelini R, Laurenzi M, Federico R
TitleTransient kinetics of polyamine oxidase from Zea mays L.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID99192698
PubMed ID10089528
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages1429-31
AuthorsBinda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A
TitleCrystallization and preliminary X-ray analysis of polyamine oxidase from Zea mays L.
Related Swiss-protO64411
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID99197292
PubMed ID10368296
JournalStructure Fold Des
Year1999
Volume7
Pages265-76
AuthorsBinda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A
TitleA 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.
Related PDB1b37,1b5q
Related Swiss-protO64411
[7]
PubMed ID10999758
JournalClin Cancer Res
Year2000
Volume6
Pages3657-61
AuthorsWallace HM, Duthie J, Evans DM, Lamond S, Nicoll KM, Heys SD
TitleAlterations in polyamine catabolic enzymes in human breast cancer tissue.
[8]
CommentsX-ray crystallography
PubMed ID11258887
JournalBiochemistry
Year2001
Volume40
Pages2766-76
AuthorsBinda C, Angelini R, Federico R, Ascenzi P, Mattevi A
TitleStructural bases for inhibitor binding and catalysis in polyamine oxidase.
Related PDB1h81,1h82,1h83,1h84,1h86

comments
According to the literature [6] and [8], this enzyme catalyzes the following reactions:
(A) Hydride transfer from N1-acetylspermine to FAD, giving an imino intermediate and FADH2:
(B) Exchange of double-bonded atoms of the imino intermediate by water, giving N1-acetylspermidine and 3-aminopropanal:
(C) Hydride transfer from FADH2 to O2, giving FAD and H2O2:

createdupdated
2004-06-032012-10-03


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.