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ENZYME entry: EC 1.5.3.13
| Accepted Name |
|---|
| N(1)-acetylpolyamine oxidase.
|
| Alternative Name(s) |
|---|
| PAO. |
| polyamine oxidase. |
| Reaction catalysed |
|---|
- H2O + N(1)-acetylspermidine + O2 <=> 3-acetamidopropanal + H2O2 + putrescine
- H2O + N(1)-acetylspermine + O2 <=> 3-acetamidopropanal + H2O2 + spermidine
|
| Comment(s) |
|---|
- The enzyme also catalyzes the reaction: N(1),N(12)-diacetylspermine +
O2 + H2O = N(1)-acetylspermidine + 3-acetamamidopropanal + H2O2.
- No or very weak activity with spermine, or spermidine in absence of
aldehydes.
- In presence of aldehydes the enzyme catalyzes the reactions: 1.
- spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with
weak efficiency 2.
- spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2.
- Found in mammalian peroxisomes and oxidizes N(1)-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, EC 1.5.3.15, EC 1.5.3.16 and
EC 1.5.3.17.
- Formerly EC 1.5.3.11, EC 1.5.3.n3, EC 1.5.3.n4 and EC 1.5.3.n10.
|
| Cross-references |
|---|
| BRENDA | 1.5.3.13 |
| EC2PDB | 1.5.3.13 |
| ExplorEnz | 1.5.3.13 |
| PRIAM enzyme-specific profiles | 1.5.3.13 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.5.3.13 |
| IUBMB Enzyme Nomenclature | 1.5.3.13 |
| IntEnz | 1.5.3.13 |
| MEDLINE | Find literature relating to 1.5.3.13 |
| MetaCyc | 1.5.3.13 |
| Rhea expert-curated reactions | 1.5.3.13 |
| UniProtKB/Swiss-Prot |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.5.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-