ISSN:
1438-2199
Keywords:
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
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00806591
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