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 FMS1 |
Enzyme Information
| 1.5.3.17 |
Non-specific polyamine oxidase.
based on mapping to UniProt P50264
(1) Spermine + O(2) + H(2)O = spermidine + 3-aminopropanal + H(2)O(2). (2) Spermidine + O(2) + H(2)O = putrescine + 3-aminopropanal + H(2)O(2). (3) N(1)-acetylspermine + O(2) + H(2)O = spermidine + 3-acetamidopropanal + H(2)O(2). (4) N(1)-acetylspermidine + O(2) + H(2)O = putrescine + 3-acetamidopropanal + H(2)O(2).
-!- The non-specific polyamine oxidases may differ from each other considerably. -!- The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N(8)-acetylspermidine. -!- The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine. -!- The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines. -!- The specific polyamine oxidases are classified as EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.15 and EC 1.5.3.16. -!- Formerly EC 1.5.3.11, EC 1.5.3.n1, EC 1.5.3.n2 and EC 1.5.3.n4.
|
UniProtKB Entries (1)
| P50264 |
FMS1_YEAST
Saccharomyces cerevisiae S288C
Polyamine oxidase FMS1
|
PDB Structure
| PDB | 4GDP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Mechanistic and Structural Analyses of the Roles of Active Site Residues in Yeast Polyamine Oxidase Fms1: Characterization of the N195A and D94N Enzymes.
Biochemistry
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