词条 | Polyamine oxidase |
释义 |
| Name = polyamine oxidase | EC_number = 1.5.3.11 | CAS_number = 294646-71-2 | IUBMB_EC_number = 1/5/3/11 | GO_code = 0046592 | image = | width = | caption = }} In enzymology, a polyamine oxidase ({{EC number|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 studiesAs of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1B37}}, {{PDB link|1H81}}, {{PDB link|1H82}}, {{PDB link|1H83}}, {{PDB link|1H84}}, {{PDB link|1H86}}, {{PDB link|1RSG}}, {{PDB link|1YY5}}, and {{PDB link|1Z6L}}. References1. ^{{cite journal|last=Moschou|first=Panagiotis|author2=Maite Sanmartin |author3=Athina H Andriopoulou |author4=Enrique Rojo |author5=Jose J Sanchez-Serrano |author6=Kalliopi A Roubelakis-Angelakis |title=Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis|journal=Plant Physiology|date=1 August 2008|volume=147|issue=4|pages=1845–1857}}
4 : EC 1.5.3|Flavin enzymes|Iron enzymes|Enzymes of known structure |
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