Abstract
Aspartate aminotransferase fromLactobacillus munnus is thermostable, its activity being not changed for two months at temperatures between 4 and - 70 áC Maximum activity was observed at 40 áC and pH 7.3 in phosphate buffer (30 mmol/L) ‡G* Value of 26.3 kJ/mol was calculated from the Arrhenius plot TheK m values for L aspartate and 2 oxoglutarate at pH 7.3 were 25 and 100 mmol/L, respectively Sodium maleate and gluta mate acted as inhibitors of the enzyme activity TheK 1 values for sodium maleate with L aspartate of 2 oxoglutarate as variable substrates were 1.1 and 0.5 mmol/L, respectively TheK 1 values for glutamate with L aspartate or 2 oxoglutarate were 8.0 and 4.0 mmol/L, respectively An inhibitory effect was observed with 1 mM Hg2+ions (1 mmol/L) The activity of the enzyme was diminished by only 12 % in the absence of pyridoxal 5’ phosphate.
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This work was partially supported by grants fromSecretaría de Ciencia y Tecnología (CONIGET), República Argentina, 1985-1986.
Part II of the series Aspartate metabolism inLactobacillus murinus CNRZ313. Part I:J. Gen. Appl. Microbiol. 31, 403-409 (1985).
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Rollan, G., Manca de Nadra, M.C., Pesce de Ruiz Holgado, A. et al. Aspartate aminotransferase ofLactobacillus murinus . Folia Microbiol 33, 344–348 (1988). https://doi.org/10.1007/BF02925842
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DOI: https://doi.org/10.1007/BF02925842