Exam (elaborations)
MCBM 1- (6) Enzyme, Kinetics, and Regulation (MCBM) Questions with 100% Correct Answers
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MCBM 1- (6) Enzyme, Kinetics, and Regulation (MCBM) Questions with 100% Correct Answers
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How can enzyme activity be regulated?
Give this one a try later!
, 1) Genes can impact enzyme concentration
2) Enzymes can interact with inhibitors, allosteric interactions,
and feedback controls
3) The physical structure of the enzyme can be changed via
phosphorylation/dephosphorylation or zymogen activity
Statin competes with HMG-CoA for the active site for HMG-CoA
reductase.
Inhibitor reduces cholesterol levels in the blood because the
competitive inhibitor will take over the cholesterol binding spot.
Binds to a different spot from the active site.
DOES NOT EFFECT THE BINDING OF THE SUBSTRATE TO THE
ENZYME!
Will inactive catalysis
Vmax is decreased, Km decreases (affinity increases).
This is because unbound and bound enzymes exist in equilibrium.
When bound enzymes are essentially "removed" from the equation,
there will be a natural drive to balance this out by binding more
substrate to enzyme.
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, 2 of 20
Term
How can competitive inhibition be applied to a clinical scenario?
Give this one a try later!
Only binds to ES complex! Once it does this it will inhibit the catalytic
ability of the enzyme-substrate complex.
Statin competes with HMG-CoA for the active site for HMG-CoA
reductase.
Inhibitor reduces cholesterol levels in the blood because the
competitive inhibitor will take over the cholesterol binding spot.
1) Genes can impact enzyme concentration
2) Enzymes can interact with inhibitors, allosteric interactions, and
feedback controls
3) The physical structure of the enzyme can be changed via
phosphorylation/dephosphorylation or zymogen activity
Km will stay the same since the substrate binding is not changed.
Vmax will decrease since it stops catalysis!
Don't know?
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