Q. The active site of an enzyme remains

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Q. An enzyme and a reactant molecule maintain relationship as

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Q. An enzyme is assayed at an initial substrate concentration of 2 x 10¯⁵M. In 6 minute, half of the substrate is used. The Km for the substrate is 2 x 10¯³M. The value of k in minute is

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Q. The plot commonly used for determining the value of Vmax is

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Q. Quasi steady state is also known as

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Q. Which of these enzymes contains a Zinc (Zn) ion?

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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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