CATH Classification

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 3BNU
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis of the substrate stereospecificity of FMS1.
Huang, Q., Hao, Q.
To Be Published