#Question id: 628
#Section 2: General Biology
At fixed substrate concentration, which of the following equation is correct for Dixon plot
#Question id: 629
#Section 2: General Biology
In the presence of a fixed concentration of a competitive inhibitor, which of the following would best characterize an enzyme-catalyzed reaction when the concentration of the substrate is increased?
#Question id: 630
#Section 2: General Biology
In case of competitive inhibition, plots of Km against [Io] fixed [Eo] have
#Question id: 631
#Section 2: General Biology
Two curves showing the rate versus substrate concentration are shown below for an enzyme-catalyzed reaction. One curve is for the reaction in the presence of substance X. The other curve is for data in the absence of substance X. Examine the curves and tell which statement below is false.
#Question id: 634
#Section 2: General Biology
An enzyme has a Vmax of 50 micromol product formed (minute x mg protein)-1 and a Km of 10 microM for the substrate. When a reaction mixture contains the enzyme and 5 microM substrate, which of the following percentages of the maximum velocity will be closest to the initial reaction rate?
#Question id: 635
#Section 2: General Biology
The enymatic rate constant (kcat/Km) of orotidine 5ʹ-phosphate decarboxylase is 6 x 107 M-1s-1 and the nonenzymatic rate constant (kn) is 3 x 10-16 s-1. What is the value of the enzymeʹs catalytic proficiency?