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• W1570987914 abstract "The active site of ATP: guanidine phosphotransferases. II. Evidence for a critical histidine residue through use of a specific reagent, diethylpyrocarbonate 1. ATP-creatine phosphotransferase (EC 2.7.3.2) and ATP:l-arginine phosphotransferase (EC 2.7.3.3) are inhibited at pH 6.1 by diethylpyrocarbonate, their reactive sulfhydryl groups being reversibly masked or not. The extent of inactivation is first-order with respect to time and inhibitor concentration. The ability of the substrates, used separately or mixed, to protect arginine kinase against inhibition, suggests the involvement of the modified group in the enzymic reaction. Nevertheless, in the case of creatine kinase no protection has been observed. 2. The carbethoxylated enzymes develop a difference ultraviolet spectrum with a maximum peak at 240 mμ, a specific feature of N-carbethoxyimidazole formation. From the kinetic data of spectrophotometric titrations and loss of activity, it is concluded that one histidine residue and two histidine residues are modified per mole of arginine kinase and creatine kinase respectively, causing total inactivation. 3. Advantages of diethylpyrocarbonate as a protein-histidyl reagent are demonstrated by the specific titration of the histidine content in both denaturated enzymes. Furthermore it is shown that the number and reactivity of -SH groups are not modified in the carbethoxylated inhibited phosphokinases. 1. L'ATP:créatine phosphotransférase (EC 2.7.3.2) et l'ATP:l-arginine phosphotransférase (EC 2.7.3.3), employées sous la forme native ou après masquage de leurs groupes -SH essentiels, sont inhibées, à pH 6.1, par le pyrocarbonate d'éthyle. Le degré d'inhibition varie avec le temps et la concentration en inhibiteur. Les substrats de la réaction de transphosphorylation, employés séparément ou mélangés, protègent efficacement l'arginine kinase, mais ne sont d'aucun effet vis-à-vis de la créatine kinase. 2. Les enzymes carbéthoxylés présentent un spectre d'absorption différentiel avec un maximum d'absorption à 240 mμ, caractéristique de la formation de N-carbéthoxyimidazole. Les déterminations spectrophotométriques effectuées parallèlement aux mesures de la perte d'activité démontrent l'implication de deux résidus histidine actifs dans la créatine kinase et d'un résidu histidine essentiel dans l'arginine kinase. 3. La spécificité du pyrocarbonate d'éthyle à l'égard des résidus histidine a été mise en relief par l'étude de la carbéthoxylation de ces aminoacides dans les phosphagène kinases dénaturées. Cette spécificité a été encore soulignée par la non-modification du nombre et de la réactivité des groupes -SH dans les enzymes inhibés." @default.
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• W1570987914 date "1968-10-01" @default.
• W1570987914 modified "2023-09-27" @default.
• W1570987914 title "Site actif des ATP: Guanidine phosphotransférases" @default.
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• W1570987914 doi "https://doi.org/10.1016/0005-2744(68)90211-8" @default.
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