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Primary structure and expression of peroxisomal acetylspermidine oxidase in the methylotrophic yeast Candida boidinii

M Nishikawa1, T Hagishita, H Yurimoto

  • 1Research Institute for Biological Sciences Okayama, Okayama, Japan. mnishikawa@mth.biglobe.ne.jp

FEBS Letters
|July 29, 2000
PubMed

Insights

Researchers purified acetylspermidine oxidase (ASOD) from yeast and cloned its gene, ASO1. This study is the first to identify the gene for ASOD, an enzyme crucial for N-acetylated polyamine metabolism.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Acetylspermidine oxidase (ASOD) is an FAD-containing amine oxidase involved in polyamine metabolism.
  • It catalyzes the oxidation of N-acetylated spermidine.

Purpose of the Study:

  • To purify ASOD from Candida boidinii.
  • To clone and characterize the gene encoding ASOD.
  • To determine the substrate specificity and localization of ASOD.

Main Methods:

  • Purification of ASOD from Candida boidinii.
  • Gene cloning using polymerase chain reaction (PCR) based on partial amino acid sequences.
  • Sequence analysis of the ASO1 gene and its encoded protein.
  • Localization studies in overexpressed Candida boidinii cells.

Main Results:

  • ASOD was purified to homogeneity from Candida boidinii.
  • The enzyme specifically oxidized N(1)-acetylspermidine.
  • The ASOD-encoding gene, ASO1, was cloned. It is 1530 bp long, encoding a 509-amino acid protein (57.167 kDa).
  • ASO1 contains a FAD-binding motif and a peroxisome targeting signal 1 (PTS1).
  • ASOD was localized to peroxisomes in overexpressed cells.

Conclusions:

  • This is the first report of a gene encoding ASOD capable of oxidizing N-acetylated polyamines.
  • The characterized gene and enzyme provide insights into polyamine metabolism and peroxisomal function in yeast.

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