Polyamine oxidase
From Wikipedia, the free encyclopedia
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.
Contents |
[edit] 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.
[edit] References
- IUBMB entry for 1.5.3.11
- BRENDA references for 1.5.3.11 (Recommended.)
- PubMed references for 1.5.3.11
- PubMed Central references for 1.5.3.11
- Google Scholar references for 1.5.3.11
- Bolkenius FN, Seiler N (1981). "Acetylderivatives as intermediates in polyamine catabolism". Int. J. Biochem. 13: 287–92. doi:. PMID 7215618.
- Holtta E (1983). "Polyamine oxidase (rat liver)". Methods. Enzymol. 94: 306–11. PMID 6621391.
[edit] External links
-
- The CAS registry number for this enzyme class is 294646-71-2.
[edit] Gene Ontology (GO) codes
 |
This EC 1.5 enzyme-related article is a stub. You can help Wikipedia by expanding it. |
