S. Tanase, Y. Morino
Feb 23, 1976
Citations
1
Influential Citations
35
Citations
Quality indicators
Journal
Biochemical and biophysical research communications
Abstract
Abstract L-Propargylglycine serves as an amino acid substrate in the transamination reaction catalyzed by both cytosolic and mitochondrial aspartate aminotransferases from pig heart. Incubation of these isoenzymes with L-propargylglycine alone did not result in the inactivation of these enzymes. However, the presence of 2-oxoglutarate or pyruvate caused gradual irreversible inactivation of these isoenzymes. The inactivation was greatly accelerated by the presence of formate ion. Inactivation of both isoenzymes with L-[2- 14 C]propargylglycine resulted in stoichiometric incorporation of the radioactive molecule. Drastic changes in the absorption and circular dichroic spectra of the enzymes which took place during the inactivation also indicated that the modification by L-propargylglycine is restricted to the active site of these isoenzymes.