Exam 3 Flashcards
The two distinct divisions of metabolism
Catabolic reactions (catabolism) and anabolic reactions (anabolism)
Catabolic Reactions (characteristics)
1) Breaks down complex molecules, makes them simpler. 2) releases energy. 3) DOWNHILL REACTION
Anabolic Reactions (characteristic)
- links simple molecules
- makes them more complex
- require energy
- UPHILL REACTIONS
Metabolic Pathways
Series of chemical reactions that happen in a cell
Delta G
G (products) - G (reactants)
Delta G in exergonic reactions
Negative
Delta G in endergonic reactions
Positive
Energy coupling
Exergonic reactions are used to drive endergonic ones
ATP
Adenosine Triphosphate
“Energy currency” in cells
Powers cellular work through energy coupling
How does the release of energy occur during the hydrolysis of ATP?”
The chemical change to a lower state of free energy causes energy to be released
How do enzymes speed up metabolic reactions?
By lowering the activation energy barrier, making it so that the reaction to happen at moderate temperatures.
Catalyst
Chemical agent that speeds up a reaction without being consumed by the reaction
What is an enzyme?
A catalytic protein. (Names often end in -ase)
What is the enzyme’s substrate?
The reactant that an enzyme acts on.
What happens when the enzyme binds to its substrate?
Enzyme-substrate complex is created
What happens to the enzyme when the substrate enters the active site?
Enzyme changes shape slightly, creating an induced fit.
What affects enzyme activity?
Temperature, pH, cofactors, and inhibitors.
Temperature’s effect on enzyme activity
As temperature increases, the reaction rate will also increase. Enzymes also have a peak performance at a temperature optimum, they denature beyond that temperature.
pH’s effect on enzyme activity.
Most enzymes have a pH at which they perform at peak efficiency (pH optimum)
What is a cofactor?
A nonprotein helper that binds to the enzyme permanently, or reversibly with the substrate
What is a coenzyme?
Organic cofactors
What are inhibitors?
Chemicals that selectively inhibit the action of specific enzymes
When is inhibition usually irreversible?
When the inhibitor covalent bonds with the enzyme
When does reversible inhibition happen?
When inhibitors bind to the enzyme by weak interactions