Yeast Fms1 is a FAD-utilizing polyamine oxidase.
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.
Landry
Joseph
J
Program in Genetics, Stony Brook University, Stony Brook, NY 11794, USA.
Sternglanz
Rolf
R
D000107:Acetylation; D001483:Base Sequence; D015317:Biogenic Polyamines / Q000737:chemistry / Q000378:metabolism; D004271:DNA, Fungal / Q000235:genetics; D004875:Ergosterol / Q000096:biosynthesis; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D005800:Genes, Fungal; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity; D000097667:Polyamine Oxidase
D015317:Biogenic Polyamines; D004271:DNA, Fungal; D004875:Ergosterol; D005182:Flavin-Adenine Dinucleotide; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D000097667:Polyamine Oxidase; C108504:FMS1 protein, S cerevisiae