DB code: D00042
CATH domain | 3.50.50.60 : FAD/NAD(P)-binding domain | Catalytic domain |
---|---|---|
3.90.660.10 : Polyamine Oxidase; Chain A, domain 2 | Catalytic domain | |
E.C. | 1.5.3.14 1.5.3.15 | |
CSA | 1b5q | |
M-CSA | 1b5q | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.90.660.10 : Polyamine Oxidase; Chain A, domain 2 | T00211 |
3.50.50.60 : FAD/NAD(P)-binding domain | M00163 D00015 D00041 D00045 D00064 D00071 T00004 T00015 T00017 T00025 T00211 T00213 T00233 T00242 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
O64411 |
Polyamine oxidase
|
EC
1.5.3.n6
EC 1.5.3.n7 EC 1.5.3.n8 EC 1.5.3.n9 |
NP_001105106.1
(Protein)
NM_001111636.1 (DNA/RNA sequence) |
PF01593
(Amino_oxidase)
[Graphical View] |
KEGG enzyme name |
---|
polyamine 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 ) |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
O64411 | PAO_MAIZE | Spermidine + 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). | Monomer. | FAD. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||||||||
KEGG-id | C00016 | C00001 | C00007 | C00315 | C01029 | C00027 | C00986 | C00555 | C05936 | ||||||
E.C. |
(1.5.3.14, 1.5.3.15)
|
(1.5.3.14, 1.5.3.15)
|
1.5.3.14
|
1.5.3.15
|
(1.5.3.14, 1.5.3.15)
|
(1.5.3.14, 1.5.3.15)
|
1.5.3.14
|
1.5.3.15
|
|||||||
Compound | FAD | H2O | O2 | spermidine | N8-acetylspermidine | H2O2 | propane-1,3-diamine | 4-aminobutanal | 4-acetamidobutanal | ||||||
Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | H2O | others | amine group,lipid | amide group,amine group,lipid | others | amine group,lipid | amine group,carbohydrate,lipid | amide group,carbohydrate,lipid | ||||||
ChEBI |
16238 |
15377 |
27140 26689 15379 |
16610 |
27911 |
16240 |
15725 |
17769 |
7386 |
||||||
PubChem |
643975 |
962 22247451 |
977 |
1102 |
123689 |
784 22326046 |
428 |
118 |
440850 |
||||||
1b37A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b37B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b37C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b5qA01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b5qB01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b5qC01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h81A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h81B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h81C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h82A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h82B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h82C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h83A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h83B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h83C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h84A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h84B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h84C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h86A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h86B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h86C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b37A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b37B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b37C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b5qA02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Analogue:MD2 | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b5qB02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Analogue:MD2 | Unbound | Unbound | Unbound | Unbound | Unbound | |
1b5qC02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Analogue:MD2 | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h81A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h81B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h81C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h82A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Analogue:GZZ | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h82B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Analogue:GZZ | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h82C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Analogue:GZZ | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
1h83A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:DIA | Unbound | Unbound | Unbound | |
1h83B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:DIA | Unbound | Unbound | Unbound | |
1h83C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:DIA | Unbound | Unbound | Unbound | |
1h84A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:FAD-NBA | |
1h84B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:FAD-NBA | |
1h84C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:FAD-NBA | |
1h86A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:FAD-NBA | |
1h86B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:FAD-NBA | |
1h86C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:FAD-NBA |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [8] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1b37A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1b37B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1b37C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1b5qA01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1b5qB01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1b5qC01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h81A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h81B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h81C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h82A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h82B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h82C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h83A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h83B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h83C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h84A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h84B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h84C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h86A01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h86B01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1h86C01 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 62 | ||||
1b37A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1b37B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1b37C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1b5qA02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1b5qB02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1b5qC02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h81A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h81B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h81C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h82A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h82B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h82C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h83A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h83B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h83C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h84A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h84B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h84C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h86A02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h86B02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 | ||||
1h86C02 |
![]() |
![]() |
![]() |
![]() |
![]() |
GLU 170 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[6]
|
Fig.1(a), p.271-273 | |
[8]
|
Figure 1 | p.2767 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3181599 |
Journal | Int J Biochem |
Year | 1988 |
Volume | 20 |
Pages | 695-702 |
Authors | Tsukada T, Furusako S, Maekawa S, Hibasami H, Nakashima K |
Title | Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1654929 |
Journal | Biotechnol Appl Biochem |
Year | 1991 |
Volume | 14 |
Pages | 54-9 |
Authors | Cona A, Federico R, Gramiccia M, Orsini S, Gradoni L |
Title | The amino aldehydes produced by spermine and spermidine oxidation with maize polyamine oxidase have anti-leishmanial effect. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7503806 |
Journal | Biochem Pharmacol |
Year | 1995 |
Volume | 50 |
Pages | 1527-30 |
Authors | Libby PR, Munson BR, Fiel RJ, Porter CW |
Title | Cationic porphyrin derivatives as inhibitors of polyamine catabolism. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9210657 |
Journal | Arch Biochem Biophys |
Year | 1997 |
Volume | 343 |
Pages | 146-8 |
Authors | Bellelli A, Angelini R, Laurenzi M, Federico R |
Title | Transient kinetics of polyamine oxidase from Zea mays L. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) |
Medline ID | 99192698 |
PubMed ID | 10089528 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 1998 |
Volume | 54 |
Pages | 1429-31 |
Authors | Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A |
Title | Crystallization and preliminary X-ray analysis of polyamine oxidase from Zea mays L. |
Related PDB | |
Related UniProtKB | O64411 |
[6] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) |
Medline ID | 99197292 |
PubMed ID | 10368296 |
Journal | Structure Fold Des |
Year | 1999 |
Volume | 7 |
Pages | 265-76 |
Authors | Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A |
Title | A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. |
Related PDB | 1b37 1b5q |
Related UniProtKB | O64411 |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10999758 |
Journal | Clin Cancer Res |
Year | 2000 |
Volume | 6 |
Pages | 3657-61 |
Authors | Wallace HM, Duthie J, Evans DM, Lamond S, Nicoll KM, Heys SD |
Title | Alterations in polyamine catabolic enzymes in human breast cancer tissue. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11258887 |
Journal | Biochemistry |
Year | 2001 |
Volume | 40 |
Pages | 2766-76 |
Authors | Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A |
Title | Structural bases for inhibitor binding and catalysis in polyamine oxidase. |
Related PDB | 1h81 1h82 1h83 1h84 1h86 |
Related UniProtKB |
Comments |
---|
According to the literature [6] and [8], (A) Hydride transfer from N1-acetylspermine to FAD, (B) Exchange of double-bonded atoms of the imino intermediate by water, (C) Hydride transfer from FADH2 to O2, |
Created | Updated |
---|---|
2004-06-03 | 2012-10-03 |