Abstract

The biosynthetic enzyme L-threonine deaminase, which catalyzes the first specific step in the pathway of L-isoleucine biosynthesis, was one of the first examples of feed-back inhibition to be analyzed directly at the enzyme level. As discovered by Umbarger (1956 a, b, c; 1957) L-isoleucine, the endproduct of the chain, strongly inhibits the activity of this enzyme.

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