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- W2065600897 abstract "Transaldolase (Type III) from Candida utilis was found to be inactivated by tetranitromethane only in the presence of the substrates fructose 6-phosphate and sedoheptulose 7-phosphate. This reaction was prevented by the addition of erythrose 4-phosphate or glyceraldehyde 3-phosphate, which are known to accept dihydroxyacetone from the transaldolase-dihydroxyacetone complex, releasing free transaldolase. These results strongly suggest that tetranitromethane does not react with free transaldolase but only with the Schiff-base intermediate. After 1 min of incubation with the reagent at pH 6.0, 4 moles of nitroformate were produced per mole of inactivated enzyme. The modification, probably a nitration or an oxidation of certain amino acid residues of the complex by tetranitromethane, caused a dissociation of the dihydroxyacetone moiety from the complex without any recovery of the enzymatic activity. The fact that the reaction with tetranitromethane takes place only in the presence of substrates indicates that a substrate-mediated change of conformation occurs in transaldolase. Chemical and spectrophotometric evidence is presented showing that tetranitromethane did not modify tyrosine, cysteine, and tryptophan residues in the inactivated enzyme. From amino acid analyses it appears that histidine, serine, proline, methionine, tyrosine, and phenylalanine residues were not altered by this reagent. The possible mechanisms of modification of the transaldolasedihydroxyacetone complex and the chemical nature of the modification by tetranitromethane are discussed." @default.
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- W2065600897 title "Substrate-dependent inactivation of transaldolase activity with tetranitromethane" @default.
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- W2065600897 doi "https://doi.org/10.1016/0003-9861(72)90128-2" @default.
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