Polyamine oxidase
In enzymology, a polyamine oxidase (EC 1.5.3.11) is an enzyme that catalyzes the chemical reaction
- N1-acetylspermine + O2 + H2O N1-acetylspermidine + 3-aminopropanal + H2O2
The 3 substrates of this enzyme are N1-acetylspermine, O2, and H2O, whereas its 3 products are N1-acetylspermidine, 3-aminopropanal, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N1-acetylspermidine:oxygen oxidoreductase (deaminating). This enzyme is also called 1-N-acetylspermidine:oxygen oxidoreductase (deaminating). It has 2 cofactors: FAD, and Iron. A similar enzyme in plants catalyzes non-acetylated polyamines.[1]
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1B37, 1H81, 1H82, 1H83, 1H84, 1H86, 1RSG, 1YY5, and 1Z6L.
References
- ↑ Moschou, Panagiotis; Maite Sanmartin; Athina H Andriopoulou; Enrique Rojo; Jose J Sanchez-Serrano; Kalliopi A Roubelakis-Angelakis (1 August 2008). "Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis". plant physiology 147 (4): 1845–1857.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|