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 1B5Q
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.
Binda, C., Coda, A., Angelini, R., Federico, R., Ascenzi, P., Mattevi, A.
Structure Fold.Des.