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Module 10 Set 6

apoenzyme protein component of an enzyme
cofactor nonprotein component of an enzyme
prosthetic group firmly attached
coenzyme loosely attached
holoenzyme apoenzyme + cofactor
a typical exergonic reaction A + B → ABt → C + D
transition-state complex resembles both the substrates and the products
enzyme speeds up reaction by lowering Ea
activation energy energy required to form transition-state complex
lock-and-key model: only the substrate (key) fits into the active site (key hole) of the enzyme (lock)
induced-fit model: only the proper substrate is capable of inducing the proper alignment of the active site for the enzyme to perform its catalytic function
how enzymes lower Ea: By increasing concentrations of substrates at active site of enzyme
how enzymes lower Ea: By orienting substrates properly with respect to each other in order to form the transition-state complex
isoenzymes different enzymes that catalyze same reaction
each end product regulates the initial pacemaker enzyme
each end product regulates its own branch of the pathway
feedback inhibition also called end product inhibition
inhibition of one or more critical enzymes in a pathway regulates entire pathway
pacemaker enzyme catalyzes the slowest or rate-limiting reaction in the pathway
Created by: Whereis_raye
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