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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.

Cross-references

BRENDA

EC2PDB

ExplorEnz

PRIAM enzyme-specific profiles

KEGG Ligand Database for Enzyme Nomenclature

IUBMB Enzyme Nomenclature

IntEnz

MEDLINE

MetaCyc

UniProtKB/Swiss-Prot

Q865R1, PAOX_BOVIN;

Q6QHF9, PAOX_HUMAN;

Q8C0L6, PAOX_MOUSE;

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.

All 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.-.-.-