|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: spermine oxidase
Enzyme Commission Synonyms: PAOh1/SMO, PAOh1 (ambiguous), AtPAO1, AtPAO4, SMO, mSMO, SMO(PAOh1), SMO/PAOh1, SMO5, mSMOmu
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -21.580627 [Latendresse13]
Enzyme Commission Summary:
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 220.127.116.11 (N1-acetylpolyamine oxidase), EC 18.104.22.168 (polyamine oxidase (propane-1,3-diamine-forming)), EC 22.214.171.124 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 126.96.36.199 (non-specific polyamine oxidase).
Unification Links: Rhea:25816
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
Wang03: 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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493