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This report is concerned with the site-specific labelling of an allosteric enzyme, glutamic acid dehydrogenase (GDH). The alanine ( (hand symbol) pyruvate) site of GDH has been labelled by a substrate analog-bromo-pyruvate, resulting in the irreversible inhibition of the alanine activity but with full retention of the glutamate activity. The findings strongly suggest that the pyruvate group is covalently linked to the alanine site of the enzyme. A new method will be discussed in terms of chemical mutation and the regulatory properties of allosteric enzymes.
