D-Aspartate oxidase and D-amino acid oxidase are localised in the peroxisomes of terrestrial gastropods

Eur J Cell Biol. 2001 Oct;80(10):651-60. doi: 10.1078/0171-9335-00197.

Abstract

D-Aspartate oxidase and D-amino acid oxidase were found in high activity in the tissues of representative species of terrestrial gastropods. Analytical subcellular fractionation demonstrated that both of these oxidases co-localised with the peroxisome markers, acyl-CoA oxidase and catalase, in the digestive gland homogenate. Electron microscopy of peak peroxisome fractions showed particles of uniform size with generally well preserved variably electron-dense matrices bounded by an apparently single limiting membrane. Many of the particles exhibited a core region of enhanced electron density. Catalase cytochemistry of peak fractions confirmed the peroxisome identity of the organelles. Peroxisome-enriched subcellular fractions were used to investigate the properties of gastropod D-aspartate oxidase and D-amino acid oxidase activities. The substrate and inhibitor specificities of the two activities demonstrated that two distinct enzymes were present analogous to, but not identical to, the equivalent mammalian peroxisomal enzymes.

MeSH terms

  • Amino Acid Oxidoreductases / analysis*
  • Animals
  • Catalase / analysis
  • D-Amino-Acid Oxidase / analysis*
  • D-Aspartate Oxidase
  • Digestive System / enzymology
  • Hydrogen Peroxide
  • Oxidants
  • Peroxisomes / enzymology*
  • Snails / enzymology*
  • Subcellular Fractions / enzymology

Substances

  • Oxidants
  • Hydrogen Peroxide
  • Catalase
  • Amino Acid Oxidoreductases
  • D-Aspartate Oxidase
  • D-Amino-Acid Oxidase