A mathematical analysis of branched pathway regulation has led to the prediction of a novel homoserine control in Escherichia coli B. Experimental support for such control is presented in this paper. Homoserine, the precursor of both threonine and methionine, inhibits nicotinamide adenine dinucleotide phosphate (NADP+) specific glutamate dehydrogenase (EC 188.8.131.52), the enzyme catalyzing the first reaction in ammonia assimilation. Physiological and biochemical evidence for this effect are offered. Homoserine depresses the growth rate of the organism, and glutamate, the product of the inhibited reaction, reverses this effect. The NADP+ specific glutamate dehydrogenase activity in cell free extracts is inhibited by homoserine, and this inhibition parallels the restriction of growth rate. These effects are found in other enteric bacteria which share a similar overall pattern of control for the amino acids derived from aspartate. On the other hand, a sampling of more distantly related species which have different pathways and/or regulatory patterns provides no evidence for homoserine inhibition of the glutamate dehydrogenase reaction.
|Original language||English (US)|
|Number of pages||10|
|Journal||Journal of Bacteriology|
|State||Published - 1973|
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology