The relationship of 4-hydroxybenzoic acid to lysine and methionine formation in Escherichia coli

Abstract

A multiple aromatic mutant, E. coli 156:53D2, required 4-hydroxybenzoic acid for rapid aerobic growth on a number of carbon sources. In the absence of 4-hydroxybenzoic acid aerobic growth was stimulated by a mixture of lysine and methionine and by succinate. The influence of the amino-acids is attributed to a sparing of succinyl-CoA. Low activities of both a-oxoglutarate dehydrogenase and fumarate reductase were found in organisms grown aerobically without 4-hydroxybenzoate and consequently both mechanisms known for the formation of succinate were impaired. The low fumarate-reductase activity in these organisms was due to repression of enzyme synthesis by aeration and not to enzyme inactivation. In contrast lactate dehydrogenase and ethanol dehydrogenase were induced. This is interpreted as the appearance of alternative routes of NADH oxidation when electron transfer to oxygen is impaired. The activities of the other tricarboxylic acid-cycle enzymes tested were little influenced by 4-hydroxybenzoate deficiency, although anaerobiosis resulted in a fall in activity.