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- W2016120158 abstract "Abstract The prephenate dehydratase of Bacillus subtilis exists as an equilibrium mixture of two interconvertible proteins, 55,000 daltons and 210,000 daltons, respectively. The properties of highly purified enzyme (600-fold) are the same as those observed in crude extracts, a finding that reinforces other indications that a single gene product is involved. Positive effectors ( l -methionine, l -leucine and prephenate) favor the 210,000 molecular weight species of enzyme, while negative effectors ( l -phenylalanine and l -tryptophan) favor dissociation of the enzyme to the 55,000 molecular weight species. The use of effector mixtures shows that l -phenylalanine-mediated dissociation is strongly dominant. In contrast, positive effectors can antagonize the otherwise potent dissociating effect of l -tryptophan. Activity in crude extracts is not proportional to enzyme concentration below 2.5 mg of protein per ml owing to the concentration-dependent nature of the interconversion. Positive effectors linearize the relation between reaction velocity and enzyme concentration, while negative effectors expand the range of enzyme concentration within which disproportionality is found. The multi-metabolite control of prephenate dehydratase provides an enzymological basis for interpathway relationships of regulation that is postulated to function as a metabolite balancing mechanism. A mechanism that preserves balanced levels of hydrophobic amino acids could contribute significantly to optimizing the process of protein synthesis." @default.
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- W2016120158 date "1974-12-01" @default.
- W2016120158 modified "2023-09-25" @default.
- W2016120158 title "Metabolic interlock: Control of an interconvertible prephenate dehydratase by hydrophobic amino acids in Bacillus subtilis" @default.
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- W2016120158 doi "https://doi.org/10.1016/0022-2836(74)90235-6" @default.
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