Yeast Fms1 is a FAD-utilizing polyamine oxidase

Biochem Biophys Res Commun. 2003 Apr 11;303(3):771-6. doi: 10.1016/s0006-291x(03)00416-9.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylation
  • Base Sequence
  • Biogenic Polyamines / chemistry
  • Biogenic Polyamines / metabolism
  • DNA, Fungal / genetics
  • Ergosterol / biosynthesis
  • Flavin-Adenine Dinucleotide / metabolism
  • Genes, Fungal
  • Oxidation-Reduction
  • Oxidoreductases Acting on CH-NH Group Donors / chemistry
  • Oxidoreductases Acting on CH-NH Group Donors / genetics
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Substrate Specificity


  • Biogenic Polyamines
  • DNA, Fungal
  • FMS1 protein, S cerevisiae
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Flavin-Adenine Dinucleotide
  • Oxidoreductases Acting on CH-NH Group Donors
  • polyamine oxidase
  • Ergosterol