Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver

Hoppe Seylers Z Physiol Chem. 1978 Apr;359(4):481-8. doi: 10.1515/bchm.1978.359.1.481.


Aromatic-amino-acid-glyoxylate aminotransferase was highly purified from the mitochondrial fraction of livers from monkey and glucagon-injected rats. The two enzyme preparations showed physical and enzymic properties different from a kynurenine aminotransferase previously described. The two enzymes had nearly identical molecular weights (approximate 80 000), isoelectric points (pH 8.0) and pH optima (pH 8.0 - 8.5). However, a difference in substrate specificity was observed between the two enzymes. Both enzymes utilized glyoxylate, pyruvate, hydroxypyruvate and 2-oxo-4-methyl-thiobutyrate as effective amino acceptors. 2-Oxoglutarate was active for rat enzyme but not for monkey enzyme. With glyoxylate, amino donors were effective in the following order of activity; phenylalanine greater than histidine greater than tyrosine greater than tryptophan greater than 5-hydroxytrypotphan greater than kynurenine for the rat enzyme, and phenylalanine greater than kynurenine greater than histidine greater than tryptophan greater than 5-hydroxy-tryptophan for the monkey enzyme.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acids
  • Animals
  • Glucagon / pharmacology
  • Glyoxylates
  • Haplorhini
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Male
  • Mitochondria, Liver / enzymology*
  • Molecular Weight
  • Rats
  • Substrate Specificity
  • Transaminases / antagonists & inhibitors
  • Transaminases / isolation & purification*
  • Transaminases / metabolism


  • Amino Acids
  • Glyoxylates
  • Glucagon
  • Transaminases