|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
Enzymes and Genes:
|Arabidopsis thaliana col:||spermine oxidase: PAO1|
spermine oxidase: PAO4
non-specific polyamine oxidase: PAO3
|Homo sapiens:||polyamine oxidase 1 (spermidine-forming): SMOX|
|Saccharomyces cerevisiae:||non-specific polyamine oxidase: FMS1|
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 184.108.40.206: spermine oxidase
Enzyme Commission Synonyms for 220.127.116.11: PAOh1/SMO, PAOh1 (ambiguous), AtPAO1, AtPAO4, SMO, mSMO, SMO(PAOh1), SMO/PAOh1, SMO5, mSMOmu
Enzyme Commission Primary Name for 18.104.22.168: non-specific polyamine oxidase
Enzyme Commission Synonyms for 22.214.171.124: polyamine oxidase (ambiguous), Fms1, AtPAO3
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -21.580688 [Latendresse13]
Enzyme Commission Summary for 126.96.36.199:
The enzyme from Arabidopsis thaliana ( PAO1) oxidizes norspermine to norspermidine with high efficiency. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 188.8.131.52 (N1-acetylpolyamine oxidase), EC 184.108.40.206 (polyamine oxidase (propane-1,3-diamine-forming)), EC 220.127.116.11 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 18.104.22.168 (non-specific polyamine oxidase).
Enzyme Commission Summary for 22.214.171.124:
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [Landry03]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [Muller92a]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [Moschou08]. The specific polyamine oxidases are classified as EC 126.96.36.199 (N1-acetylpolyamine oxidase), EC 188.8.131.52 (polyamine oxidase (propane-1,3-diamine-forming)), EC 184.108.40.206 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 220.127.116.11 (spermine oxidase).
Moschou08: Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA (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 Physiol 147(4);1845-57. PMID: 18583528
MurrayStewart08: Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA (2008). "Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology." FEBS J 275(11);2795-806. PMID: 18422650
Tavladoraki06: Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R (2006). "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion." Plant Physiol 141(4);1519-32. PMID: 16778015
Wang03a: Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO." Biochem Biophys Res Commun 304(4);605-11. PMID: 12727196
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493