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• W1520381577 abstract "The active site of ATP: guanidine phosphotransferases. I. Reaction of the essential ε-NH2 lysine groups with i-dimethylaminonaphthalene-5-sulphonylchloride 1. ATP: creatine phosphotransferase (EC 2.7.3.2) and ATP: l-arginine phosphotransferase (EC 2.7.3.3) are specifically inhibited by i-dimethylaminonaphthalene-5-sulfonylchloride, their essential sulphydryl groups being reversibly masked. The metal complexes Mg-ATP and Mg-ADP are shown to increase the inactivation rate of creatine kinase only. 2. The yellow fluorescent dye-labelled enzymes exhibit a characteristic absorption spectrum with an absorption maximum at 335 mμ. The extent of inhibition is in good agreement with the different degrees of labelling, a fact which suggests that the dye has reacted at an enzymatically active site. Complete loss of activity is associated with the binding of two moles of dansyl per mole of creatine kinase and with one mole of dye per mole of arginine kinase. 3. High voltage electrophoresis and thin-layer chromatography of the single fluorescent derivative isolated after pronase digestion of the dansylated enzymes led to the identification of ε-DNS-lysine; these data provide evidence that the residue affected in both proteins is a lysine side chain. 1 L'ATp:créatine phosphotransférase (EC2.7.3.2) et l'ATP:arginine phosphotransférase (EC 2.7.3.3) sont spécifiquement inhibées par le i-diméthylaminonaphtalène-5-sulfochlorure, après protection réversible de leurs groupes SH essentiels. 2 L'étude spectrophotomètriquw des protéines dansylées, purifiées, montre que la pete d'activité est associée à l'incorporation de deux moles de dansyl par mole de créatine kinase et d'une mole de DNS par mole d'arginine kinase. 3 Le site fixation du chromophore dans chaque protéine a été identifié comme étant la ε-NH2-lysine." @default.
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• W1520381577 date "1968-10-01" @default.
• W1520381577 modified "2023-09-27" @default.
• W1520381577 title "Site actif des ATP: Guanidine phosphotransférases" @default.
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• W1520381577 doi "https://doi.org/10.1016/0005-2744(68)90210-6" @default.
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