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- W2000495172 abstract "Abstract 1. 1. Procedures are described for the selection of two classes of presumptive structural gene mutants of the 3-deoxy- d -arabino-heptulosonate 7-phosphate synthase (7-phospho-2-keto-3-deoxy- d -arabino-heptonate d -erythrose-4-phosphate-lyase (pyruvate-phosphorylating), EC 4.1.2.15) (DAHP synthase) of the fungus Neurospora crassa. (a) Three separate activity-negative mutations have been correlated with isoenzymes inhibited by the end products, tyrosine, phenylalanine and tryptophan; arom-6 with DAHP synthase (Tyr), arom-7 with DAHP synthase (Phe) and arom-8 with DAHP synthase (Trp). (b) Mutants retaining activity but no longer allosterically inhibited (allosteric inhibition-negative) were obtained for each of the three isoenzymes. 2. 2. Arom-6, arom-7 and arom-8 are unlinked to the “arom gene cluster”. Arom-6 maps on linkage group VI L; arom-7 and arom-8 both map on linkage group I R but are widely separated. Therefore, no DAHP synthase operon or operon-like gene cluster exists. In all three cases, the absence of recombination and complementation in vitro (enzymic) and in vivo (forced heterocaryon) indicates that the two classes of mutations associated with a specific isoenzyme are allelic. On this hypothesis a single polypeptide prescribes activity and allosteric inhibition, but the polypeptide is different for each isoenzyme. 3. 3. Strains carrying arom-6 and grown in the presence of phenylalanine, tyrosine and tryptophan have a nutritional requirement for the folic acid precursor 4-aminobenzoate. This suggests that DAHP synthase (Tyr) plays a special regulatory role associated with the synthesis of 4-aminobenzoate. 4. 4. It is concluded that DAHP synthase is differentially controlled by phenylalanine, tyrosine and tryptophan without channelling of DAHP." @default.
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- W2000495172 date "1969-08-01" @default.
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- W2000495172 title "Studies concerning the biochemical genetics and physiology of activity and allosteric inhibition mutants of Neurospora crassa 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase" @default.
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- W2000495172 doi "https://doi.org/10.1016/0005-2744(69)90436-7" @default.
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