The Reversal by Organic Mercurials of "allosteric" Changes in Glutamate Dehydrogenase.

“Allosteric” (1) reagents are thought to affect the catalytic activity and state of aggregation of glutamate dehydrogenase CL glutamate : NAD (P) oxidoreductase (deaminating), EC 1.4.1.3) by binding at noncatalytic sites and changing the structure of the protein (2-7). Reaction of the enzyme with organic mercurials reduces its sensitivity to these reagents (4, 8), alters the pH-activity curve of the glutamate dehydrogenase reaction, and inhibits the alanine dehydrogenase reaction catalyzed by the enzyme (9). The effects of the mercurials have been discussed in terms of a scheme involving three different interconvertible forms of the enzyme (6).