Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.

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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

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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	Yes	Ligand	Details

Polypeptides

Name	UniProt ID
Spermine oxidase	Q9NWM0	Details