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- W2003140964 abstract "Anthranilate synthase and anthranilate-5′-phosphoribosyl-1-pyrophosphate phosphoribosy transferase (PR Transferase) enzymatic activities related to tryptophan biosynthesis in Aerobacter aerogenes purify together as an enzyme aggregate. Anthranilate synthase converts chorismate into anthranilate. The formation of anthranilate is conveniently followed by examining the fluorescence of anthranilate. An assay based on the ultraviolet absorption of anthranilate may also be used. Anthranilate synthase assays are effectively used to follow the purification of the anthranilate synthase-PR transferase aggregate. This assay is convenient for kinetic studies and is linear over the period of observation. In assay for PR Transferase activity, the reaction is measured by following the disappearance of anthranilate fluorometrically. The product is less fluorescent than anthranilate and very unstable and therefore not isolated. One unit of anthranilate synthase activity is the amount catalyzing the formation of 0.1 micromole of anthranilate in 20 minutes at 37º. A mixture of ribose 5-phosphate and adenosine triphosphate (ATP) does not substitute for phosphoribosyl pyrophosphate (PRPP) in the purified preparation. Mg2+ is required as a cofactor." @default.
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- W2003140964 date "1961-01-01" @default.
- W2003140964 modified "2023-09-22" @default.
- W2003140964 title "Evidence for the enzymatic synthesis of N-(5′-phosphoribosyl) anthranilic acid, a new intermediate in tryptophan biosynthesis" @default.
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- W2003140964 doi "https://doi.org/10.1016/0006-291x(61)90261-3" @default.
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