Amino Acids

, Volume 10, Issue 2, pp 187–196 | Cite as

d-Aspartyl residue in a peptide can be liberated and metabolized by pig kidney enzymes

  • Y. Kera
  • K. Funabashi
  • T. Matsumoto
  • T. Watanabe
  • H. Nagasaki
  • R. Yamada


The presence of an enzyme activity which hydrolyzes glycyl-d-aspartate was found in the homogenates of pig kidney cortex. The activity was inhibited by metal chelating agents and cilastatin, suggesting that the enzyme was a cilastatin-sensitive metallo-peptidase. Of the two hydrolysis products,d-aspartate was found to be less accumulated than glycine. The fate ofd-aspartate was, therefore, examined and the amino acid was found to be converted tol-aspartate,l-alanine and pyruvate, in the presence ofl-glutamate. Experiments with enzyme inhibitors suggested that the conversion involvedd-aspartate oxidase, aspartate aminotransferase and alanine aminotransferase as well as decarboxylation of oxaloacetate produced fromd-aspartate. All the results indicate that the enzymes in the pig kidney can liberate thed-aspartyl residue in the peptide and convert it to the compounds readily utilizable. The finding suggests a probable metabolic pathway of thed-aspartate-containing peptide.


Amino acids Hydrolysis of glycyl-d-aspartate d-Aspartyl residue in peptides Metallo-enzyme Conversion ofd-aspartate tol-amino acids d-Aspartate oxidase Aspartate aminotransferase Alanine aminotransferase 


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Copyright information

© Springer-Verlag 1996

Authors and Affiliations

  • Y. Kera
    • 1
  • K. Funabashi
    • 1
  • T. Matsumoto
    • 1
  • T. Watanabe
    • 1
  • H. Nagasaki
    • 2
  • R. Yamada
    • 1
  1. 1.Department of BioEngineeringNagaoka University of TechnologyNagaoka, NiigataJapan
  2. 2.Department of Food Science and NutritionDoshisha Women's College of Liberal ArtsKyotoJapan

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