Feb 1, 1976

Derepression of certain aromatic amino acid biosynthetic enzymes of Escherichia coli K-12 by growth in Fe3+-deficient medium

Journal of Bacteriology
J W McCray, K M Herrmann

Abstract

3-Deoxy-arabino-heptulosonic acid 7-phosphate synthase, prephenate dehydratase, tryptophan synthase, and 2,3-dihydroxybenzoylserine synthase enzyme activities are derepressed in wild-type Escherichia coli K-12 cells grown on Fe3+-deficient medium. This derepression is reversed when FeSO4 is added to the growth medium. Addition of shikimic acid to the Fe3+-deficient growth medium caused repression of the first three enzyme activities but not of 2,3-dihydroxybenzoylserine synthase activity. Addition of 2,3-dihydroxybenzoic acid to the Fe3+-deficient growth medium has no effect on any of the above-mentioned enzyme activities. The Fe3+ deficiency-mediated derepression of 3-deoxyarabino-heptulosonic acid 7-phosphate synthase activity is due to an elevation of the tyrosine-sensitive isoenzyme; the phenylalanine-sensitive isoenzyme is not derepressed under these conditions.

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Mentioned in this Paper

Tryptophan Synthase
Shikimic Acid
Alkalescens-Dispar Group
Aldehyde-Lyases
2-Dehydro-3-Deoxyphosphoheptonate Aldolase
Prephenate Dehydratase
Hydroxybenzoates
PMS-Tryptophan
Endorphenyl
Hydro-Lyases

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