Enzymes and Kinetics Questions

• The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is
• A noncompetitive inhibitor of an enzyme-catalyzed reaction
• Quasi steady state is also known as
• The plot commonly used for determining the value of Vmax is
• An allosteric inhibitor of an enzyme usually
• In competitive inhibition a factor is obtained from the measurement of
• The reciprocal equation for non competitive inhibition can be arranged to the equation for the
• The relationship between Keq, Km and Vmax is known as
• The types of inhibition pattern based on Michaelis Menten equation are
• Which of the following activity is possible by transferases?
• Which of the following common drugs is not a specific enzyme inhibitor?
• Which of the following statements is not true?
• Which of the following statements is true for enzymatically catalyzed reaction?
• The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by
• A classical uncompetitive inhibitor is a compound that binds
• Which of these proteases is not a cysteine active site protease?
• A competitive inhibitor of an enzyme is usually
• 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
• An enzyme and a reactant molecule maintain relationship as
• Linear inhibition is sometimes called as