A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 1.5.3.13
Accepted Name |
N(1)-acetylpolyamine oxidase.
|
Alternative Name(s) |
PAO. |
Polyamine oxidase. |
Reaction catalysed |
- N(1)-acetylspermidine + O(2) + H(2)O <=> putrescine + 3-acetamidopropanal + H(2)O(2)
- N(1)-acetylspermine + O(2) + H(2)O <=> spermidine + 3-acetamidopropanal + H(2)O(2)
|
Cofactor(s) |
FAD.
|
Comment(s) |
- The enzyme also catalyzes the reaction: N(1),N(12)-diacetylspermine +
O(2) + H(2)O = N(1)-acetylspermidine + 3-acetamamidopropanal +
H(2)O(2).
- No or very weak activity with spermine, or spermidine in absence of
aldehydes.
- In presence of aldehydes the enzyme catalyzes the reactions: 1.
- spermine + O(2) + H(2)O = spermidine + 3-aminopropanal + H(2)O(2),
and with weak efficiency 2.
- spermidine + O(2) + H(2)O = putrescine + 3-aminopropanal + H(2)O(2).
- 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.
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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 |
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.-.-.-