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- W1533456777 abstract "Abstract The effect of a number of chemically reactive inhibitors on the selective inactivation of formylglycinamide ribonucleotide amidotransferase has been studied. Reagents are described that selectively abolish the utilization of glutamine as a nitrogen source while affecting NH4Cl utilization in a definite manner. The stoichiometry of binding to the enzyme has been determined for 14C-iodoacetate and 14C-iodoacetamide. A glutamine analogue, 14C-albizziin (NH2-14CONHCH2CHNH2COOH), was shown to bind covalently in a ratio of 1 mole per mole of active enzyme with a molecular weight of 133,000. The albizziin-modified enzyme was inactive when assayed with glutamine but was fully active when NH4Cl was used as the nitrogen source. Hydroxylamine, N-methylhydroxylamine, and potassium cyanate were also found to inactivate formylglycinamide ribonucleotide amidotransferase by reaction at the γ-glutamyl site." @default.
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- W1533456777 date "1969-11-01" @default.
- W1533456777 modified "2023-10-11" @default.
- W1533456777 title "Biosynthesis of the Purines" @default.
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- W1533456777 doi "https://doi.org/10.1016/s0021-9258(18)63553-7" @default.
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