CATH Classification

Domain Context

CATH Clusters

Superfamily FAD/NAD(P)-binding domain
Functional Family Polyamine oxidase 1

Enzyme Information

1.5.3.15
N(8)-acetylspermidine oxidase (propane-1,3-diamine-forming).
based on mapping to UniProt O64411
N(8)-acetylspermidine + O(2) + H(2)O = propane-1,3-diamine + 4-acetamidobutanal + H(2)O(2).
-!- Also active with N(1)-acetylspermine, weak activity with N(1),N(12)- diacetylspermine. -!- No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. -!- Absence of monoamine oxidase (EC 1.4.3.4) activity. -!- Differs in specificity from EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.16 and EC 1.5.3.17. -!- Formerly EC 1.5.3.11, EC 1.5.3.n6, EC 1.5.3.n7, EC 1.5.3.n8 and EC 1.5.3.n9.
1.5.3.14
Polyamine oxidase (propane-1,3-diamine-forming).
based on mapping to UniProt O64411
Spermidine + O(2) + H(2)O = propane-1,3-diamine + 4-aminobutanal + H(2)O(2).
-!- As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines. -!- Catalyzes less efficiently the oxidation of N(1)-acetylspermine and spermine. -!- Differs in specificity from EC 1.5.3.13, 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.n6, EC 1.5.3.n7, EC 1.5.3.n8 and EC 1.5.3.n9.

UniProtKB Entries (1)

O64411
PAO1_MAIZE
Zea mays
Polyamine oxidase 1

PDB Structure

PDB 3KPF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The crystal structure of the mutant K300M of polyamine oxidase from ZEA MAYS unveils the role of LYS300 in catalysis
Fiorillo, A., Ilari, A., Tavladoraki, P.
To be Published