inhibition Flashcards
draw chemical equation of competitive inhibition
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draw competitive inhibition graph
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characteristics of competitive inhibition
- competes with substrate for active site
- I binds to E
- affects Km, does not affect Vmax or kcat
- reduces [E]
- raise [S] to reverse the effect
why doesn’t competitive inhibition affect kcat?
why does competitive inhibition apparently affect [S]?
competitive inhibition math equation
v = (Vmax [S]) / aKm + [S]
a = alpha = weighting factor
uncompetitive inhibition, draw graph
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draw chem equation for uncompetitive inhibition
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math equation uncompetitive inhibition
v = Vmax[S] / Km + a’[S]
uncompetitive inhibition characteristics
- I binds ES
- affect Vmax, Km and kcat
- binding at a different site causes distortion in the active site
- [S] «< Km, small [ES], therefore effect of UI id negligable
why is Vmax not reversed by increasing [S] in uncompetitive inhibition?
If you increase the concentration os S, more ES complexes will form, which means there are more opportunities or EIS to form, rather than product.
Instead, lowering the subtrate concentration will allow more EP to form rather than EIS
What is the difference between allosteric inhibitors and uncompetitive inhibition?
UI only binds to ESm while ASI could bind to E or ES, and it is also based on a different kinetic model
How does uncompetitive inhibition modify both kcat (Vmax and Km?
Draw MI/noncompetitive inhibition chemical equation
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draw MI/noncompetitive inhibition graph
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