1887

Abstract

Aspartate aminotransferase (EC 2.6.1.1) and alanine aminotransferase (EC 2.6.1.2) were extracted from mycelia of , partially purified and characterized. The pH optima for the enzyme activities were 9·0 and 8·6, respectively. Both enzymes were relatively stable at 37 °C but rapidly denatured at 60 °C. They were inducible by both -aspartate and -alanine, but aspartate was the better inducer. The apparent Michaelis constants for aspartate aminotransferase when -aspartate and 2-oxoglutarate were used were 7·14 m and 1·32 m, respectively. In the case of alanine aminotransferase, using -alanine and 2-oxoglutarate the corresponding values were 8·33 m and 1·85 m, respectively. The enzymes were competitively inhibited by succinate with values of 21 m and 17 m for aspartate aminotransferase and alanine aminotransferase, respectively. Both enzymes could use -methionine whereas only aspartate aminotransferase could use -tyrosine as amino donor.

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1980-10-01
2021-10-24
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