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_____ describes when a cofactor is covalently bound to an enzyme.
Prosthetic group
______ experiences cooperativity.
Hemoglobin
If Km value of an enzyme is elevated, then the _____.
substrate does not bind to the enzyme well
Km is the ______.
Substrate concentration at half of the maximum rate of a catalyzed reaction
A drug can inhibit a substrate by mimicking its structure & binding to its enzyme’s active site. What is occurring?
competitive inhibition
In order to counteract competitive inhibition, what can be done?
Increase substrate concentration
What occurs during competitive inhibition of an enzyme?
Substance mimics a substrate and inhibits the enzyme by binding at the active site
Vmax is unchanged
Km increases
What occurs during non-competitive inhibition of an enzyme?
inhibitor binds to enzyme’s allosteric site, reaction does not get catalyzed
Vmax decreases
Km is unchanged
Which biological molecule makes up enzymes?
Amino acids
If biding affinity is high, then Km is ____.
low
Vmax is the ___.
max rate of an enzyme catalyzed reaction
If Km value of an enzyme is low, what is occuring?
Enzyme requires a relatively low substrate concentration to reach ½ Vmax
If a reaction has a +^G value, then _____.
the reaction is endergonic (require an input of energy to occur)
the reaction in non spontaneous
The ability to drive a secondary active transport can be explained by _____.
Gibbs free energy
What is an example of how potential energy is stored in the biological systems?
The chemical bonds b/w phosphate groups in an ATP molecule
How are non-spontaneous reactions driven forward in biological systems?
Reaction coupling
True or false: ATP’s bonds b/w its phosphate groups are high energy
True
True or false: ATP can be used to power non-spontaneous chemical reactions
True
True or false: ATP is a nucleotide
True
True or false: ATP hydrolysis is a highly endergonic reaction
False
True or false: The formation of ATP from ADP requires energy to occur
True
True or false: Catalysts can lower the activation energy of the reaction
True
True or false: Catalysts can stabilize the transition state
True
True or false: Catalysts can make non-spontaneous reactions spontaneous
False
True or false: Catalysts can provide an alternative pathway
True
True or false: Catalysts can be reused, as they are not consumed in the reaction
True
Enzyme-substrate complexes are held together via_____.
Weak, temporary bonds
What best describes cofactors and how they are involved in enzyme catalysis?
Cofactors can bind covalently or non-covalently to the enzyme
True or false: Zymogens help with enzyme regulation
True
True or false: All zymogens are proenzymes
True
True or false: Zymogens can be activated through cleavage
True
True or false: Zymogens are active biological catalysts
False
Pepsinogen is a zymogen found in the human stomach
True
What effects enzyme function and regulation?
pH, chemical modification, temperature, gene expression
What does not effect enzyme function and regulation?
free energy
How can the Vmax of an enzyme can be increased?
Increasing the enzyme concentration
What may affect the Km of an enzyme?
Competitive inhibition
What decreases the Vmax of an enzyme?
Non-competitive inhibition
What is true regarding the Gibbs free energy of cellular respiration?
^H-T^S has ne negative value (makes a reaction favorable)
ATP is an unstable molecule because ____.
it has 3 negatively charged phosphate groups
What is Q10?
It measures how sensitive reaction rates are to temperature changes
Q10 temperature coefficient equation
Q10 = (K2/K1)^(10/t2-t1)
Examples of hydrolases
Lipase
Peptidase
Nuclease
Amylase
_____are enzymes that break down molecules using water (via hydrolysis).
Hydrolases
Chymotrypsin
Pepsin
Trypsin
All of these enzymes are involved in protein digestion
____ is an enzyme that is responsible for breaking down starch into maltose.
Amylase
A researcher needs to cut a circular plasmid at a specific DNA sequence in the middle of the strand. What enzyme should be used to make this cut?
Endonuclease