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- W1966692735 abstract "Two 3-deoxy-d-arabino-heptulosonic acid 7-phosphate (DAHP) synthetases, one of which is inhibited by tyrosine and the other by phenylalanine, exist in Escherichia coli mutant 83-24. The abilities of a number of analogs of phenylalanine and tyrosine to substitute for the natural metabolites in preventing the synthesis of or inhibiting the activity of the two DAHP synthetases have been examined. It can be concluded that the enzymatic sites to which phenylalanine and tyrosine must conform on the respective DAHP synthetases are relatively specific. An unsubstituted 4-position of the aromatic ring enhances binding of an analog in place of phenylalanine, and for effective binding in lieu of tyrosine, a 4-hydroxyl group greatly increases binding affinity of an analog. For prevention of enzyme synthesis, a variety of analogs are appreciably active, indicating that the structural requirements for repression are somewhat less specific than the requirements for regulation of the activity of the DAHP synthetases. Some effects of these inhibitors have been correlated with their ability to prevent growth of the parent organism, Escherichia coli W." @default.
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- W1966692735 date "1964-05-01" @default.
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- W1966692735 title "The effects of phenylalanine and tyrosine analogs on the synthesis and activity of 3-deoxy-d-arabino-heptulosonic acid 7-phosphate synthetases" @default.
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- W1966692735 doi "https://doi.org/10.1016/0003-9861(64)90026-8" @default.
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