a protein catalyst that speeds up a chemical reaction
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red
Which line (red or blue) represents an enzyme catalyzed reaction?
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blue
Which line (red or blue) represents an uncatalyzed reaction?
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progress of reaction
What is the x-axis of this graph?
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energy
What is the y-axis of this graph?
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activation energy
What is the "hill" of this graph called?
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decrease
Does an enzyme increase or decrease the activation energy of a reaction?
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substrate
the reactant in an enzyme catalyzed reaction
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active site
the region on the enzyme where the substrate binds
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active site
What is the arrow pointing at?
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products
What is the arrow pointing at?
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reaction rate
a measure of how fast an enzyme catalyzed reaction occurs
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enzyme activity
another word for reaction rate
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optimum conditions
the temperature and pH where enzyme activity is highest
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denaturation
destruction of the active site of the enzyme by breaking the weak bonds of the secondary, tertiary, and quaternary structures
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denaturation/loss of 3D Shape
What has happened to this protein?
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high temperatures or changes in pH
What are two environmental factors that can denature a protein?
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inhibitor
prevents the substrate from binding to the enzyme, decreasing enzyme activity
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competitive inhibitor
binds to the enzyme at the active site and blocks the substrate from binding
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competitive inhibitor
What kind of inhibitor is this?
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noncompetitive inhibitor
binds to the enzyme somewhere other than the active site and changes the shape of the active site
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noncompetitive inhibitor
What kind of inhibitor is this?
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enzyme concentration
What is the x-axis on this graph?
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enzyme activity
What is the y-axis on this graph?
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pH
What is the x-axis on this graph?
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enzyme activity
What is the y-axis on this graph?
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optimum pH
What does the green x represent?
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substrate concentration
What is the x-axis on this graph?
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enzyme activity
What is the y-axis on this graph?
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point of saturation
What does the green x represent?
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temperature
What is the x-axis on this graph?
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optimum temperature
What does the green x represent?
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catabolic pathways
Series of reactions that release energy by breaking down complex molecules into simpler compounds.
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anabolic pathways
Series of reactions that consume energy to build complicated molecules from simpler ones.
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free energy
Measures the portion of a system's energy that can perform work when temperature and pressure are uniform throughout the system, as in a living cell.
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endergonic
Reaction that absorbs free energy from its surroundings.
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exergonic
Reaction that proceeds with a net release of free energy.
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energy coupling/ATP couples...
The use of an exergonic process to drive an endergonic one.
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catalyst
A chemical agent that speeds up a reaction without being consumed by the reaction.
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enzyme substrate complex
When an enzyme binds to its substrate, it forms:
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coenzymes and cofactors
What are two types of activators?
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Cofactor
inorganic compound example heme
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Coenzyme
Non-protein Organic helpers, example thiamin and vitamin B1
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competitive inhibitors
Reduce the productivity of enzymes by blocking substrates from entering active sites.
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noncompetitive inhibitors
Impede enzymatic reactions by binding to another part of the enzyme (other than the active site) allosteric site and changes the structure of the active site
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by lowering the activation energy required for the reaction to occur
How do enzymes catalyze reactions?
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Temperature, pH and Concentration of the Substrate
An enzyme's activity can be affected by what three factors?
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Breakdown of H2O2
What reaction does catalase catalyze?
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activation and inhibition
What kinds of regulation exist for enzymes?
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turn on the enzyme
What does activation do?
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turn off the enzyme
What does inhibition do?
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competitive and allosteric
What are the two types of inhibition?
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What is another name for allosteric inhibition?
noncompetitive inhibition
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The reactants or the product amounts
How do you measure the rate of an enzymatic reaction?
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lock and key
What is the interaction between the active site and the substrate like?
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they speed up reactions and lower the activation energy necessary to catalyze them
What is the advantage for using an enzyme?
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the allosteric site
Where does a noncompetitive inhibitor bind?
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changes the shape of the active site, by bonding to the allosteric site
What does a noncompetitive inhibitor do?
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phosphorylation
the released phosphate moves to another molecule to give energy
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induced fit
enzymes will change the shape of their active site to allow the substrate to bind better
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allosteric activator
substrate binds to ONE active site and stabilizes the shape of the enzyme so that the active sites remain OPEN
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allosteric inhibitor
substrate binds to allosteric site and stabilizes the shape of the enzyme so that the active sites are CLOSED (inactive form)
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cooperatively
substrate binds to one active site (on an enzyme with more than one active site) which stabilizes the active form CONSIDERED ALLOSTERIC REGULATION SINCE BINDING AT ONE SITE CHANGES THE SHAPE OF OTHER SITES
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feedback inhibition
The end product of a metabolic pathway can act as an inhibitor to an early enzyme in the same pathway