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- W1569227382 abstract "Abstract Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18–20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations. The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2–7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the Km for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (Ki = 31 μM) was a slightly more effective inhibitor than phenylalanine (Ki = 37 μM) at 1 m m chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l -isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis." @default.
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- W1569227382 date "1974-09-01" @default.
- W1569227382 modified "2023-09-26" @default.
- W1569227382 title "Regulation of aromatic amino acid biosynthesis in higher plants" @default.
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- W1569227382 doi "https://doi.org/10.1016/0003-9861(74)90011-3" @default.
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