Abstract
Imidazolylacetolphosphate aminotransferase (EC 2.6.1.9) is essential for the biosynthesis of the amino acid L-histidine, is coded for by the C gene of the histidine operon, and its rate of synthesis can be altered by controlling the expression of the histidine operon. Synthesis of the aminotransferase during derepression of the histidine operon has been studied in a pyridoxineless strain of S. typhimurium , suspended in growth media containing or lacking pyridoxine. Our results indicate that under both sets of nutritional conditions, synthesis of enzymes from genes on either side of the C gene are normal, that synthesis of aminotransferase protein is normal and that the proposed obligatory role of the cofactor pyridoxal phosphate in the synthesis of wild-type aminotransferase protein is not substantiated.
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