Abstract
1-Thioglycerol (TG) stimulates the synthesis of porphyrin in aerobically growing Escherichia coli. Here the levels of delta-aminolevulinate biosynthetic enzymes in untreated and TG-treated E. coli THU and PUC2 (a mutant of THU which overproduces porphyrins in the presence of thiols) cells were determined. TG treatment elevated the activity of glutamyl-tRNA reductase in both strains. The increased activity was not caused by activation of preexisting enzymes by thiols or by oxidizing agents but was dependent on new protein synthesis.
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