BCH 369 chapter 7 Test with Questions Solved
100% Correct | Latest Update
diffusion controlled limit - Answer The theoretical maximum rate of an enzymatic
reaction in solution, about 10^8 to 10^9 M^-1 * s^-1
catalytic perfection - Answer A state achieved by an enzyme that operates at the
diffusion-controlled limit.
Lineweaver-Burk plot - Answer A rearrangement of the michaelis menton
equation that permits the determination of KM and Vmax from a linear plot.
bisubstrate reaction - Answer An enzyme-catalyzed reaction involving two
substrates.
random mechanism - Answer A multisubunit reaction without a compulsory order
of substrate binding to the enzyme.
ordered mechanism - Answer A multisubunit reaction with a compulsory order of
substrate binding to the enzyme.
Ping pong mechanism - Answer An enzymatic reaction in which one or more
products are released before all the substrates have bound to the enzyme.
allosteric enzyme - Answer 1
cooperativity - Answer 2
, rational drug design - Answer The synthesis of more effective drugs based on
detailed knowledge of the target molecule's structure and function.
pharmacokinetics - Answer The behavior of a drug in the body, including its
metabolism and excretion.
clinical trial - Answer A three-phase series of tests of a drug's safety and
effectiveness in human subjects.
Irreversible inhibitor - Answer A molecule that binds to and permanently
inactivates an enzyme.
suicide substrate - Answer A molecule that chemically inactivates an enzyme only
after undergoing part of the normal catalyric reaction.
competitive inhibition - Answer A form of enzyme inhibition in which a substance
competes with the substrate for binding to the enzyme active site and thereby
appears to increase Km.
inhibition constant (KI) - Answer The dissociation constant for the complex
between an enzyme and a reversible inhibitor.
EI complex - Answer The noncovalent complex that forms between an enzyme
and a reversible inhibitor.
100% Correct | Latest Update
diffusion controlled limit - Answer The theoretical maximum rate of an enzymatic
reaction in solution, about 10^8 to 10^9 M^-1 * s^-1
catalytic perfection - Answer A state achieved by an enzyme that operates at the
diffusion-controlled limit.
Lineweaver-Burk plot - Answer A rearrangement of the michaelis menton
equation that permits the determination of KM and Vmax from a linear plot.
bisubstrate reaction - Answer An enzyme-catalyzed reaction involving two
substrates.
random mechanism - Answer A multisubunit reaction without a compulsory order
of substrate binding to the enzyme.
ordered mechanism - Answer A multisubunit reaction with a compulsory order of
substrate binding to the enzyme.
Ping pong mechanism - Answer An enzymatic reaction in which one or more
products are released before all the substrates have bound to the enzyme.
allosteric enzyme - Answer 1
cooperativity - Answer 2
, rational drug design - Answer The synthesis of more effective drugs based on
detailed knowledge of the target molecule's structure and function.
pharmacokinetics - Answer The behavior of a drug in the body, including its
metabolism and excretion.
clinical trial - Answer A three-phase series of tests of a drug's safety and
effectiveness in human subjects.
Irreversible inhibitor - Answer A molecule that binds to and permanently
inactivates an enzyme.
suicide substrate - Answer A molecule that chemically inactivates an enzyme only
after undergoing part of the normal catalyric reaction.
competitive inhibition - Answer A form of enzyme inhibition in which a substance
competes with the substrate for binding to the enzyme active site and thereby
appears to increase Km.
inhibition constant (KI) - Answer The dissociation constant for the complex
between an enzyme and a reversible inhibitor.
EI complex - Answer The noncovalent complex that forms between an enzyme
and a reversible inhibitor.
