Q. Non-competitive inhibitor of an enzyme catalyzed reaction

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Q. In competitive inhibition a factor is obtained from the measurement of

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Q. Which of these proteases is not a cysteine active site protease?

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Q. Given an enzyme with a Km = 10m M and Vmax = 100 m mol/min. If [S] = 100 m M, which of the following will be true?

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Q. The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by

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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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