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.
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UniProtKB Entries (1)
P50264 |
FMS1_YEAST
Saccharomyces cerevisiae S288C
Polyamine oxidase FMS1
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PDB Structure
PDB | 3CND |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structure of fms1 in complex with N1-AcSpermine
TO BE PUBLISHED
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