WITH ANSWERS ALL REVISED AND
UPDATED
Michaelis-Menten equation - Answer-A mathematical expression that describes the
activity of an enzyme in terms of the substrate concentration ([S]), the enzyme's
maximal velocity (Vmax), and its michaelis constant (Km): Vo = Vmax [S]/(Km + [S]).
catalytic constant (Kcat) - Answer-The ratio of the maximal velocity (Vmax) of an
enzyme-catalyzed reaction to the enzyme concentration. Also called a turnover number.
Turnover number - Answer-see catalytic constant.
Kcat/Km - Answer-The apparent second-order rate constant for an enzyme catalyzed
reaction; it indicates the enzymes overall catalytic efficiency.
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.
negative effector - Answer-A substance that diminishes an enzyme's activity through
allosteric inhibition.
positive effector - Answer-A substance that boosts an enzyme's activity through
allosteric activation.
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