Photochemical inactivation of Aeromonas aminopeptidase by 2,3-butanedione.
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چکیده
منابع مشابه
Inactivation of Escherichia coli L-threonine dehydrogenase by 2,3-butanedione. Evidence for a catalytically essential arginine residue.
Incubation of homogeneous preparations of L-threonine dehydrogenase from Escherichia coli with 2,3-butanedione, 2,3-pentanedione, phenylglyoxal, or 1,2-cyclohexanedione causes a time- and concentration-dependent loss of enzymatic activity; plots of log percent activity remaining versus time are linear to greater than 90% inactivation, indicative of pseudo-first order inactivation kinetics. The ...
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The inactivation of E. coli asparaginase by 2,3-butanedione studied with L-asparagine and diazooxonorvaline as substrates obeys pseudo first order kinetics. Activity losses are linear with respect to arginine and histidine modification, with complete inactivation being correlated with alteration of one arginine and one histidine per subunit. The rate of inactivation of the enzyme was reduced in...
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The aim of this work was to test the proposal that the active site of pyrophosphate:fructose 6-phosphate 1-phosphotransferase (PFP) contains an essential arginyl residue. Enzyme activity was inhibited equally in the glycolytic and gluconeogenic directions by arginine-modifying reagents. The second-order rate constants for 2,3-butanedione and phenylglyoxal were 13.1 [plus or minus] 0.45 and 55.3...
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Glucose 6-phosphate dehydrogenase (G6PD) was purified from Streptomyces aureofaciens and inactivated with butanedione and diethylpyrocarbonate. Incubation of the enzyme with butanedione resulted in a rapid activity loss (80%) within 5 min, followed by a slow phase using a molar ratio to enzyme concentration of 100. Fluorescence studies showed a conformational change in the butanedione-modified ...
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Proton-translocating ATPase (H(+)-ATPase) was purified from mung bean (Vigna radiata L.) roots. Treatment of this enzyme with the arginine-specific reagent 2,3-butanedione in the presence of borate at 37 degrees C (pH 7.0), caused a marked decrease in its activity. Under this condition, half-maximal inhibition was brought about by 20 millimolar 2,3-butanedione at 12 minutes. MgATP and MgADP, th...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 257 4 شماره
صفحات -
تاریخ انتشار 1982