Q. When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about

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Q. A classical noncompetitive inhibitor has

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Q. The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site

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Q. Enzymes are basically

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Q. Which of the following refers to pseudo steady state ?

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Q. The slope of Lineweaver Burk plot for Michaelis Menten equation is

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Q. The initial velocity, V0, of an enzyme catalyzed reaction reaches Vmax as

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Q. The usual method(s) to solve rate equation of simple enzyme kinetics is/are

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Q. Michaelis Menten equation can also be written as

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Q. Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?

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Q. Most enzymes work by

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Q. Which category of enzymes belongs to class 5 in the international classification?

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Q. Lock and key theory is based on the compatibility of

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Q. When an enzyme is functioning at Vmax, the rate of the reaction is limited by

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Q. The equation for the rate of product formation for simple enzyme reaction is given by (Where rmax, maximum reaction rate, Cs substrate concentration, Cp product concentration ES, CES enzyme-substrate concentration)

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Q. The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known as

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Q. If a reaction occurs in the absence of inhibitor with rate ν0 and in the presence of inhibitor with rate νi, the degree of inhibition is defined as

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Q. The rate equation in competitive inhibition based on Michaelis Menten equation is given by

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Q. Classical noncompetitive inhibition is obtained only under

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Q. In the steady state the material balance equation for any component of a system is

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