Yeast Fms1 is a FAD-utilizing polyamine oxidase

被引：54

作者：

Landry, J

Sternglanz, R ^{[1
]}

机构：

[1] SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA

[2] SUNY Stony Brook, Genet Program, Stony Brook, NY 11794 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 303卷 / 03期

关键词：

FMS1; polyamine oxidase; FAD; spermine; 3-aminopropanal;

D O I：

10.1016/S0006-291X(03)00416-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：771 / 776

页数：6

共 18 条

[1] THE STABILITY OF THE ORTHO-PHTHALALDEHYDE-2-MERCAPTOETHANOL DERIVATIVES OF AMINO-ACIDS - AN INVESTIGATION USING HIGH-PRESSURE LIQUID-CHROMATOGRAPHY WITH A PRECOLUMN DERIVATIZATION TECHNIQUE [J].