Publications

• Yeast Fms1 is a FAD-utilizing polyamine oxidase.

  Landry J., Sternglanz R.

  In this report we show that recombinant Saccharomyces cerevisiae Fms1 protein is a polyamine oxidase that binds FAD with an FAD:Fms1 stoichiometry of 1:1. Biochemical characterization of Fms1 shows that it can oxidize spermine, N(1)-acetylspermine, N(1)-acetylspermidine, and N(8)-acetylspermidine, ... >> More

  In this report we show that recombinant Saccharomyces cerevisiae Fms1 protein is a polyamine oxidase that binds FAD with an FAD:Fms1 stoichiometry of 1:1. Biochemical characterization of Fms1 shows that it can oxidize spermine, N(1)-acetylspermine, N(1)-acetylspermidine, and N(8)-acetylspermidine, but not spermidine. The products of spermine oxidation are spermidine and 3-aminopropanal. A kinetic analysis revealed that spermine, N(1)-acetylspermine, and N(1)-acetylspermidine are oxidized with similar efficiencies, while N(8)-acetylspermidine is a poor substrate. The data support a previous report, suggesting that Fms1 is responsible for the production of beta-alanine from spermine for the synthesis of pantothenic acid. << Less

  Biochem. Biophys. Res. Commun. 303:771-776(2003) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.

• Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine.

  Shukla O.P., Muller S., Walter R.D.

  Polyamine oxidase plays a key role in the catabolism of polyamines and regeneration of spermidine and putrescine. The mammalian enzyme utilises N1-acetylspermidine, and N8-acetylspermidine, although formed in the mammals, is not catabolised further. We have characterised an enzyme from Acanthamoeb ... >> More

  Polyamine oxidase plays a key role in the catabolism of polyamines and regeneration of spermidine and putrescine. The mammalian enzyme utilises N1-acetylspermidine, and N8-acetylspermidine, although formed in the mammals, is not catabolised further. We have characterised an enzyme from Acanthamoeba culbertsoni which acts preferentially on N8-acetylspermidine. The highly unstable enzyme was stabilised in the presence of glycerol or dimethylsulphoxide together with spermine and purified 400-fold by a combination of DEAE-cellulose, CM-cellulose, spermine-Sepharose and Sephacryl S-300 chromatography. The enzyme has a pH optimum of 8 and a temperature optimum of 45 degrees C. The relative activities on different substrates are: N8-acetylspermidine 100%, N1-acetylspermine 40%, N1-acetylspermidine 1%, N1,8-diacetylspermidine 1% and N1,12-diacetylspermine 15%. Free polyamines and substrates of monoamine oxidase were not attacked. The enzyme yielded diaminopropane as an end product of catabolism and could be involved in the biosynthesis of this unusual polyamine present in large amounts in this organism. << Less

  Mol Biochem Parasitol 51:91-98(1992) [PubMed] [EuropePMC]