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Metabolism
Totality of an organism’s chemical reactions
Metabolic pathway
Begins with specific molecule and ends in product
Catabolic pathway
Release energy by breaking down complex molecules
Anabolic pathways
Consume energy to build complex molecules
Energy
Capacity to cause change
Isolated system
Unable to exchange energy or matter with surroundings
Open system
Energy and matter can be transferred between system and surroundings
First law of thermodynamics
Energy of the universe is constant
Second law of thermodynamics
Every energy transfer or transformation increases the entropy of the universe
Entropy
Measure of molecular disorder or randomness
Spontaneous process
Occurs without energy input
Nonspontaneous processes
Occurs only if energy is provided, decrease entropy
Exergonic
Net release of free energy, spontaneous
Endergonic
Absorbs free energy from surroundings, nonspontaneous
ATP
Cell’s energy shuttle
Catalyst
Speeds up a reaction
Enzyme
Catalytic protein
Activation energy
“Jump start” to make a reaction begin
Substrate
Reactant that an enzyme acts upon
Cofactor
Nonprotein enzyme helpers
Competitive inhibitor
Bind to an active site
Noncompetitive inhibitor
Bind to another part of an enzyme
Allosteric regulation
Either inhibit or stimulate enzyme’s activitt
Feedback inhibition
End product of a metabolic pathway shuts down the pathway
How do inhibitors affect enzymatic activity?
Inhibitors disrupt an enzyme’s function
Which of the following statements describes a central role that ATP plays in cellular metabolism?
ATP provides energy coupling between exergonic and endergonic reactions.
A decrease in entropy is associated with which type of reaction?
Dehydration
Which of the following statements about anabolic pathways is true?
They consume energy to build up polymers from monomers
Which of the following statements is a logical consequence of the second law of thermodynamics?
Each chemical reaction in an organism must increase the total entropy of the universe
How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction?
By binding to an allosteric site, thus changing the shape of the active site of the enzyme
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