Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.
Article Details
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Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA Jr
Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.
Biochem Biophys Res Commun. 2003 May 16;304(4):605-11.
- PubMed ID
- 12727196 [ View in PubMed]
- Abstract
The discovery of an inducible oxidase whose apparent substrate preference is spermine indicates that polyamine catabolism is more complex than that originally proposed. To facilitate the study of this enzyme, the purification and characterization of the recombinant human PAOh1/SMO polyamine oxidase are reported. Purified PAOh1/SMO oxidizes both spermine (K(m)=1.6 microM) and N(1)-acetylspermine (K(m)=51 microM), but does not oxidize spermidine. The purified human enzyme also does not oxidize eight representative antitumor polyamine analogues; however, specific oligamine analogues were found to be potent inhibitors of the oxidation of spermine by PAOh1/SMO. The results of these studies are consistent with the hypothesis that PAOh1/SMO represents a new addition to the polyamine metabolic pathway that may represent a new target for antineoplastic drug development.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Spermine Spermine oxidase Protein Humans YesLigandDetails - Polypeptides
Name UniProt ID Spermine oxidase Q9NWM0 Details