CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
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 | 3L1R |
| 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
To be Published
|
