Abstract
Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits.
Highlights
Yeast transketolase is known to be active in the progress curves when the reaction is initiated by adding the dimeric state
The Hill plots for a wide range of thiamin-PP concentrations (Fig. 1) show that negative cooperativity exists with both Mg2` and Ca2', since Hill coefficients of 0.61 and 0.69, respectively, were obtained
Hysteretic processes are observed in systems in which an enzyme can exist in two forms with different physical and kinetic properties and with a rate of interconversion within the time scale of the assay method
Summary
THE SLOW RECONSTITUTION OF THE HOLOENZYME IS DUE TO RATE-LIMITING DIMERIZATION OF THE SUBUNITS*. The lag period varied with thiamin-PP concentration but was unaffected by preincubation of the enzyme with thiamin-PP unless the substrate was present. Similar results were obtained with ylase has not been thoroughly studied with respect to thiaminpyruvate decarboxylase at pH 6.2 except that
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